Stub1

Functionⁱ

E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. 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. 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. 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 (PubMed:23973223). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Likely mediates polyubiquitination and downregulates 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 (By similarity). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity).By similarity3 Publications

Catalytic activityⁱ

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆-ubiquitinyl-[acceptor protein]-L-lysine.2 Publications

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functionⁱ

chaperone binding Source: MGI
enzyme binding Source: MGI
G-protein coupled receptor binding Source: MGI
heat shock protein binding Source: MGI
Hsp70 protein binding
Source: HGNC
Inferred from sequence or structural similarityⁱ
- 10330192
Hsp90 protein binding Source: BHF-UCL
kinase binding Source: MGI
misfolded protein binding Source: MGI
protein binding, bridging
Source: HGNC
Traceable author statementⁱ
- 16307917
protein homodimerization activity
Source: HGNC
Inferred from direct assayⁱ
- 16307917
SMAD binding Source: HGNC
TPR domain binding
Source: HGNC
Inferred from sequence or structural similarityⁱ
- 10330192
ubiquitin protein ligase activity
Source: MGI
Inferred from direct assayⁱ
- 21855799
ubiquitin protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 21855799
ubiquitin-protein transferase activity Source: UniProtKB
ubiquitin-ubiquitin ligase activity
Source: MGI
Inferred from direct assayⁱ
- 11435423

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to heat Source: MGI
cellular response to hypoxia Source: MGI
cellular response to misfolded protein
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21855799
DNA repair Source: UniProtKB-KW
endoplasmic reticulum unfolded protein response
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 12150907
negative regulation of protein binding
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 12150907
negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
positive regulation of chaperone-mediated protein complex assembly Source: MGI
positive regulation of proteasomal ubiquitin-dependent protein catabolic process
Source: HGNC
Inferred from sequence or structural similarityⁱ
- 10330192
positive regulation of protein ubiquitination
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 12150907
positive regulation of ubiquitin-protein transferase activity
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 12150907
proteasome-mediated ubiquitin-dependent protein catabolic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21855799
protein autoubiquitination Source: UniProtKB
protein folding
Source: HGNC
Traceable author statementⁱ
- 16307917
protein K63-linked ubiquitination Source: UniProtKB
protein maturation
Source: HGNC
Traceable author statementⁱ
- 16307917
protein polyubiquitination
Source: MGI
Inferred from direct assayⁱ
- 11435423
protein quality control for misfolded or incompletely synthesized proteins
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21855799
protein ubiquitination Source: MGI
regulation of glucocorticoid metabolic process
Source: HGNC
Inferred from sequence or structural similarityⁱ
- 10330192
regulation of protein stability Source: MGI
response to ischemia Source: MGI
ubiquitin-dependent ERAD pathway Source: MGI
ubiquitin-dependent protein catabolic process
Source: ARUK-UCL
Inferred from mutant phenotypeⁱ
- 18292230
ubiquitin-dependent SMAD protein catabolic process Source: HGNC

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

Reactomeⁱ	R-MMU-2173788 Downregulation of TGF-beta receptor signaling R-MMU-8863795 Downregulation of ERBB2 signaling R-MMU-8939902 Regulation of RUNX2 expression and activity R-MMU-8948751 Regulation of PTEN stability and activity R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayⁱ	UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: STIP1 homology and U box-containing protein 1Curated (EC:2.3.2.272 Publications) Alternative name(s): Carboxy terminus of Hsp70-interacting protein1 Publication E3 ubiquitin-protein ligase CHIPCurated RING-type E3 ubiquitin transferase CHIPCurated
Gene namesⁱ	Name:Stub1Imported Synonyms:Chip1 Publication
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 17

Organism-specific databases

MGIⁱ	MGI:1891731 Stub1

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	2	K → R: Impaired interaction with ATXN3; when associated with R-4 and R-7. 1 Publication	1
Mutagenesisⁱ	4	K → R: Impaired interaction with ATXN3; when associated with R-2 and R-7. 1 Publication	1
Mutagenesisⁱ	7	K → R: Impaired interaction with ATXN3; when associated with R-2 and R-4. 1 Publication	1
Mutagenesisⁱ	261	H → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication	1
Mutagenesisⁱ	270	P → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000106330	1 – 304	STIP1 homology and U box-containing protein 1Add BLAST		304

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Cross-linkⁱ	2	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	20	PhosphoserineCombined sources	1
Cross-linkⁱ	23	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	24	PhosphoserineCombined sources	1
Modified residueⁱ	26	PhosphoserineCombined sources	1
Modified residueⁱ	150	PhosphoserineBy similarity	1
Cross-linkⁱ	222	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	256	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	274	PhosphoserineBy similarity	1

Post-translational modificationⁱ

Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3.1 Publication

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9WUD1
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9WUD1
PaxDbⁱ	Q9WUD1
PeptideAtlas More...PeptideAtlasⁱ	Q9WUD1
PRIDEⁱ	Q9WUD1

PTM databases

iPTMnetⁱ	Q9WUD1
PhosphoSitePlusⁱ	Q9WUD1

Expressionⁱ

Inductionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000039615 Expressed in 39 organ(s), highest expression level in brain
CleanExⁱ	MM_STUB1
Genevisibleⁱ	Q9WUD1 MM

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:16307917). Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DNAAF4 and POLB (By similarity). Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity (PubMed:16307917). Interacts (when monoubiquitinated) with ATXN3 (PubMed:21855799). Interacts with UBE2W (PubMed:21855799). Interacts with DNAJB6 (By similarity). Interacts with FOXP3 (PubMed:23973223). Interacts with FLCN and HSP90AA1. Interacts with HSP90. Interacts with UBE2N and UBE2V1. Interacts (via TPR repeats) with the C-terminal domains of HSPA8 and HSPA1A. Interacts with the non-acetylated form of HSPA1A and HSPA1B. Interacts with SMAD3 and HSP90AB1 (By similarity). Interacts with UBE4B (By similarity).By similarity3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Ilk	O55222	7	EBI-773027,EBI-6690138
LRRK2	Q5S007	2	EBI-773027,EBI-5323863	From Homo sapiens.
UBE2N	P61088	2	EBI-773027,EBI-1052908	From Homo sapiens.

GO - Molecular functionⁱ

chaperone binding Source: MGI
enzyme binding Source: MGI
G-protein coupled receptor binding Source: MGI
heat shock protein binding Source: MGI
Hsp70 protein binding
Source: HGNC
Inferred from sequence or structural similarityⁱ
- 10330192
Hsp90 protein binding Source: BHF-UCL
kinase binding Source: MGI
misfolded protein binding Source: MGI
protein binding, bridging
Source: HGNC
Traceable author statementⁱ
- 16307917
protein homodimerization activity
Source: HGNC
Inferred from direct assayⁱ
- 16307917
SMAD binding Source: HGNC
TPR domain binding
Source: HGNC
Inferred from sequence or structural similarityⁱ
- 10330192
ubiquitin protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 21855799

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	207969, 46 interactors
Database of interacting proteins More...DIPⁱ	DIP-29751N
IntActⁱ	Q9WUD1, 16 interactors
Molecular INTeraction database More...MINTⁱ	Q9WUD1
STRINGⁱ	10090.ENSMUSP00000040431

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	27 – 39	Combined sources	13
Helixⁱ	43 – 56	Combined sources	14
Helixⁱ	61 – 73	Combined sources	13
Helixⁱ	77 – 90	Combined sources	14
Helixⁱ	95 – 107	Combined sources	13
Helixⁱ	111 – 127	Combined sources	17
Helixⁱ	135 – 152	Combined sources	18
Helixⁱ	161 – 178	Combined sources	18
Turnⁱ	179 – 181	Combined sources	3
Helixⁱ	183 – 185	Combined sources	3
Turnⁱ	186 – 188	Combined sources	3
Helixⁱ	191 – 194	Combined sources	4
Helixⁱ	196 – 218	Combined sources	23
Helixⁱ	230 – 232	Combined sources	3
Turnⁱ	235 – 237	Combined sources	3
Beta strandⁱ	242 – 246	Combined sources	5
Beta strandⁱ	252 – 254	Combined sources	3
Helixⁱ	255 – 264	Combined sources	10
Turnⁱ	270 – 272	Combined sources	3
Helixⁱ	278 – 280	Combined sources	3
Helixⁱ	285 – 298	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9WUD1
SMRⁱ	Q9WUD1
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9WUD1

EvolutionaryTraceⁱ

Q9WUD1

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	27 – 60	TPR 1Add BLAST	34
Repeatⁱ	61 – 94	TPR 2Add BLAST	34
Repeatⁱ	96 – 128	TPR 3Add BLAST	33
Domainⁱ	227 – 301	U-boxAdd BLAST	75

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	14 – 19	Poly-Gly		6

Domainⁱ

The U-box domain is required for the ubiquitin protein ligase activity.1 Publication

The TPR domain is essential for ubiquitination mediated by UBE2D1.By similarity

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	KOG4642 Eukaryota ENOG410ZC2R LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00730000110724
HOGENOMⁱ	HOG000163725
HOVERGENⁱ	HBG053046
InParanoidⁱ	Q9WUD1
KEGG Orthology (KO) More...KOⁱ	K09561
OMAⁱ	TNATYFT
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0FJB
PhylomeDBⁱ	Q9WUD1
TreeFamⁱ	TF313937

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit 3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR013026 TPR-contain_dom IPR011990 TPR-like_helical_dom_sf IPR019734 TPR_repeat IPR003613 Ubox_domain IPR013083 Znf_RING/FYVE/PHD
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04564 U-box, 1 hit
SMARTⁱ	View protein in SMART SM00028 TPR, 3 hits SM00504 Ubox, 1 hit
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
PROSITEⁱ	View protein in PROSITE PS50005 TPR, 3 hits PS50293 TPR_REGION, 1 hit PS51698 U_BOX, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9WUD1-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY 
        60         70         80         90        100
GRAITRNPLV AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF 
       110        120        130        140        150
LGQCQLEMES YDEAIANLQR AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS 
       160        170        180        190        200
IEERRIHQES ELHSYLTRLI AAERERELEE CQRNHEGHED DGHIRAQQAC 
       210        220        230        240        250
IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL MREPCITPSG 
       260        270        280        290        300
ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW 

VEDY

Length:304

Mass (Da):34,909

Last modified:November 1, 1999 - v1

Checksum:ⁱ18BD2728908025A8

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	20	S → T in BAB22329 (PubMed:16141072).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF129086 mRNA Translation: AAD33401.1 AK002752 mRNA Translation: BAB22329.1 AK004464 mRNA Translation: BAB23315.1 AK045776 mRNA Translation: BAC32489.1 AK166630 mRNA Translation: BAE38905.1 BC027427 mRNA Translation: AAH27427.1 BC038939 mRNA Translation: AAH38939.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS28533.1
NCBI Reference Sequences More...RefSeqⁱ	NP_062693.1, NM_019719.3
UniGeneⁱ	Mm.277599 Mm.491120

Genome annotation databases

Ensemblⁱ	ENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615
GeneIDⁱ	56424
KEGGⁱ	mmu:56424
UCSC genome browser More...UCSCⁱ	uc008bcf.1 mouse

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9WUD1	E3 ubiquitin-protein ligase CHIP	)	HUMAN		303	UniRef90_Q9UNE7
STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase		PANTR		303
E3 ubiquitin-protein ligase CHIP		MACMU		303
STIP1 homology and U-box containing protein 1		PONAB		303
STIP1 homology and U-box containing protein 1		CERAT		303
+99

Protein	Similar proteins		Species	Score	Length	Source
Q9WUD1	E3 ubiquitin-protein ligase CHIP	)	HUMAN		303	UniRef50_Q9UNE7
STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase		PANTR		303
E3 ubiquitin-protein ligase CHIP		MACMU		303
STIP1 homology and U-box containing protein 1		PONAB		303
STIP1 homology and U-box containing protein 1		CERAT		303
+126

Entry informationⁱ

Entry nameⁱ	CHIP_MOUSE
Accessionⁱ	Q9WUD1Primary (citable) accession number: Q9WUD1 Secondary accession number(s): Q9DCJ0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
	Last sequence update:	November 1, 1999
	Last modified:	September 12, 2018
	This is version 168 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9WUD1 (CHIP_MOUSE)

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STIP1 homology and U box-containing protein 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Endoplasmic reticulum

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Compositional bias

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ