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. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). 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). 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 (PubMed:24613385). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609).13 Publications

Miscellaneous

Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients.

Catalytic activityⁱ

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.11
  "CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation."
  Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hoehfeld J., Patterson C.
  J. Biol. Chem. 276:42938-42944(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH HSPA8; UBE2D1; UBE2D2 AND UBE2D3.
- Ref.13
  "Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase."
  Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M., Patterson C., Pratt W.B., Osawa Y.
  J. Biol. Chem. 279:52970-52977(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
EC:2.3.2.27

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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

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

Enzyme and pathway databases

BRENDAⁱ	2.3.2.B10 2681
Reactomeⁱ	R-HSA-2173788 Downregulation of TGF-beta receptor signaling R-HSA-8863795 Downregulation of ERBB2 signaling R-HSA-8939902 Regulation of RUNX2 expression and activity R-HSA-8948751 Regulation of PTEN stability and activity R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkⁱ	Q9UNE7
SIGNORⁱ	Q9UNE7
UniPathwayⁱ	UPA00143

Protein family/group databases

MoonDBⁱ	Q9UNE7 Predicted

MoonDBⁱ

Q9UNE7 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: E3 ubiquitin-protein ligase CHIPCurated (EC:2.3.2.272 Publications) Alternative name(s): Antigen NY-CO-71 Publication CLL-associated antigen KW-81 Publication Carboxy terminus of Hsp70-interacting protein1 Publication RING-type E3 ubiquitin transferase CHIPCurated STIP1 homology and U box-containing protein 1Imported
Gene namesⁱ	Name:STUB1Imported Synonyms:CHIP1 Publication ORF Names:PP1131Imported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [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 › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 16

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11427 STUB1
MIMⁱ	607207 gene
neXtProtⁱ	NX_Q9UNE7

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR16 is characterized by truncal and limb ataxia resulting in gait instability. Additionally, patients may show dysarthria, nystagmus, spasticity of the lower limbs, and mild peripheral sensory neuropathy.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_072348	28	E → K in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. 1 Publication	1
Natural variantⁱVAR_072349	65	N → S in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination. 1 PublicationCorresponds to variant dbSNP:rs690016544EnsemblClinVar.	1
Natural variantⁱVAR_071293	79	A → D in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777347EnsemblClinVar.	1
Natural variantⁱVAR_071294	79	A → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777346EnsemblClinVar.	1
Natural variantⁱVAR_071295	123	L → V in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777344EnsemblClinVar.	1
Natural variantⁱVAR_071296	130	N → I in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777341EnsemblClinVar.	1
Natural variantⁱVAR_072350	145	K → Q in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs146251364EnsemblClinVar.	1
Natural variantⁱVAR_071297	147	W → C in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777342EnsemblClinVar.	1
Natural variantⁱVAR_071298	165	L → F in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777340EnsemblClinVar.	1
Natural variantⁱVAR_071299	236	S → T in SCAR16. 1 Publication	1
Natural variantⁱVAR_071300	240	M → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777345EnsemblClinVar.	1
Natural variantⁱVAR_071301	246	T → M in SCAR16; inhibits ubiquitin ligase activity and autoubiquitination. 2 PublicationsCorresponds to variant dbSNP:rs587777343EnsemblClinVar.	1

Spinocerebellar ataxia 48 (SCA48)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA48 is an autosomal dominant neurodegenerative disease characterized by onset in mid-adulthood of progressive cognitive decline and gait ataxia, and vermian and hemispheric cerebellar atrophy.

Related information in OMIM

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	30	K → A: Loss of interaction with FOXP3 and its ability to ubiquitinate FOXP3. Loss of interaction with SMAD3, HSPA8, HSP90AA1 and HSP90AB1. 2 Publications	1
Mutagenesisⁱ	260	H → Q: Loss of ability to ubiquitinate FOXP3. 1 Publication	1
Mutagenesisⁱ	269	P → A: Abolishes E3 ligase activity. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10273
MalaCards human disease database More...MalaCardsⁱ	STUB1
MIMⁱ	615768 phenotype 618093 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000103266
Orphanetⁱ	412057 Autosomal recessive cerebellar ataxia due to STUB1 deficiency
PharmGKBⁱ	PA36227

Miscellaneous databases

Pharosⁱ	Q9UNE7 Tbio

Pharosⁱ

Q9UNE7 Tbio

Polymorphism and mutation databases

BioMutaⁱ	STUB1
DMDMⁱ	78099173

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000106329	1 – 303	E3 ubiquitin-protein ligase CHIPAdd BLAST		303

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	19	PhosphoserineCombined sources1 Publication	1
Cross-linkⁱ	22	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	23	PhosphoserineCombined sources	1
Modified residueⁱ	25	PhosphoserineCombined sources	1
Modified residueⁱ	149	PhosphoserineCombined sources	1
Cross-linkⁱ	221	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	255	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	273	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 (By similarity). Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2.By similarity2 Publications

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9UNE7
jPOSTⁱ	Q9UNE7
MassIVEⁱ	Q9UNE7
PaxDbⁱ	Q9UNE7
PeptideAtlas More...PeptideAtlasⁱ	Q9UNE7
PRIDEⁱ	Q9UNE7
ProteomicsDBⁱ	85282 [Q9UNE7-1] 85283 [Q9UNE7-2]

PTM databases

iPTMnetⁱ	Q9UNE7
PhosphoSitePlusⁱ	Q9UNE7
SwissPalmⁱ	Q9UNE7

Expressionⁱ

Tissue specificityⁱ

Expressed in differentiated myotubes (at protein level) (PubMed:17369820). Highly expressed in skeletal muscle, heart, pancreas, brain and placenta (PubMed:10330192, PubMed:11435423). Detected in kidney, liver and lung (PubMed:10330192, PubMed:11435423).3 Publications

Inductionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000103266 Expressed in lateral nuclear group of thalamus and 226 other tissues
ExpressionAtlasⁱ	Q9UNE7 baseline and differential
Genevisibleⁱ	Q9UNE7 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB037202 CAB037209 HPA041222 HPA043531

HPAⁱ

CAB037202
CAB037209
HPA041222
HPA043531

Interactionⁱ

Subunit structureⁱ

Homodimer (By similarity).

Interacts with BAG2 (PubMed:16169850).

Interacts with E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (PubMed:11557750). Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1 (PubMed:15215316).

Interacts with MKKS (PubMed:18094050).

Interacts with DNAAF4 (PubMed:19423554).

Interacts with POLB (PubMed:19713937).

Interacts (when monoubiquitinated) with ATXN3.

Interacts with UBE2W.

Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity (By similarity).

Interacts with DNAJB6 (PubMed:22366786).

Interacts with FOXP3 (PubMed:23973223).

Interacts with FLCN (PubMed:27353360).

Interacts with HSP90AA1 (PubMed:27353360, PubMed:24613385).

Interacts with HSP90 (PubMed:11146632).

Interacts with UBE2N and UBE2V1 (PubMed:16307917).

Interacts (via TPR repeats) with the C-terminal domain of HSPA1A (PubMed:10330192).

Interacts with the non-acetylated form of HSPA1A and HSPA1B (PubMed:27708256).

Interacts (via TPR repeats) with the C-terminal domain of HSPA8 (PubMed:10330192, PubMed:11557750, PubMed:23990462, PubMed:27708256).

Interacts with SMAD3 and HSP90AB1 (PubMed:24613385).

Interacts with UBE4B (PubMed:17369820).

Interacts with RIPK3 (PubMed:29883609).

By similarity17 Publications

Binary interactionsⁱ

Entry	#Exp.	IntAct	Notes
A8K1F4	2	EBI-357085,EBI-9357094
Q96AP0	2	EBI-357085,EBI-717666
P31749	5	EBI-15687717,EBI-296087
Q86WG3	4	EBI-357085,EBI-1783328
Q99933	2	EBI-357085,EBI-1030678
O95816	4	EBI-357085,EBI-355275
O95817	3	EBI-357085,EBI-747185
Q9NRJ3	3	EBI-357085,EBI-7783254
Q8WXU2-2	3	EBI-357085,EBI-9381887
P00533	3	EBI-357085,EBI-297353
Q9BZS1	7	EBI-357085,EBI-983719
P07900	9	EBI-357085,EBI-296047
P08238	5	EBI-357085,EBI-352572
P08107	5	EBI-357085,EBI-629985
P11142	8	EBI-357085,EBI-351896
P11142-1	4	EBI-15687717,EBI-351908
Q5S007	4	EBI-357085,EBI-5323863
Q9Y2U5	9	EBI-357085,EBI-357393
P10636	5	EBI-15687717,EBI-366182
Q96PB7	3	EBI-357085,EBI-10292253
Q9BVN2	3	EBI-357085,EBI-6257312
Q99757	3	EBI-357085,EBI-2932492
P61088	5	EBI-357085,EBI-1052908
Q7Z7E8	3	EBI-357085,EBI-1783287
P12504	2	EBI-357085,EBI-779991	From Human immunodeficiency virus type 1 group M subtype B (isolate NY5).

Show more details

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	115563, 422 interactors
CORUMⁱ	Q9UNE7
Database of interacting proteins More...DIPⁱ	DIP-29752N
IntActⁱ	Q9UNE7, 165 interactors
Molecular INTeraction database More...MINTⁱ	Q9UNE7
STRINGⁱ	9606.ENSP00000219548

Miscellaneous databases

RNActⁱ	Q9UNE7 protein

RNActⁱ

Q9UNE7 protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	26 – 38	Combined sources	13
Helixⁱ	42 – 55	Combined sources	14
Helixⁱ	60 – 72	Combined sources	13
Helixⁱ	76 – 89	Combined sources	14
Helixⁱ	94 – 106	Combined sources	13
Helixⁱ	110 – 126	Combined sources	17
Helixⁱ	134 – 149	Combined sources	16

Show more details

3D structure databases

SMRⁱ	Q9UNE7
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	26 – 59	TPR 1Add BLAST	34
Repeatⁱ	60 – 93	TPR 2Add BLAST	34
Repeatⁱ	95 – 127	TPR 3Add BLAST	33
Domainⁱ	226 – 300	U-boxAdd BLAST	75

Domainⁱ

The U-box domain is required for the ubiquitin protein ligase activity.By similarity

The TPR domain is essential for ubiquitination mediated by UBE2D1.1 Publication

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	KOG4642 Eukaryota ENOG410ZC2R LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000151045
HOGENOMⁱ	CLU_056455_1_0_1
InParanoidⁱ	Q9UNE7
KEGG Orthology (KO) More...KOⁱ	K09561
OMAⁱ	QEAATCY
Database of Orthologous Groups More...OrthoDBⁱ	1422450at2759
PhylomeDBⁱ	Q9UNE7
TreeFamⁱ	TF313937

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit 3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR041312 CHIP_TPR_N 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 PF18391 CHIP_TPR_N, 1 hit 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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9UNE7-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG 
        60         70         80         90        100
RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL 
       110        120        130        140        150
GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI 
       160        170        180        190        200
EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI 
       210        220        230        240        250
EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI 
       260        270        280        290        300
TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV 

EDY

Length:303

Mass (Da):34,856

Last modified:October 25, 2005 - v2

Checksum:ⁱ7E7D6568B17070BF

GO

Isoform 2 (identifier: Q9UNE7-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-72: Missing.

« Hide

        10         20         30         40         50
MQQHEQALAD CRRALELDGQ SVKAHFFLGQ CQLEMESYDE AIANLQRAYS 
        60         70         80         90        100
LAKEQRLNFG DDIPSALRIA KKKRWNSIEE RRIHQESELH SYLSRLIAAE 
       110        120        130        140        150
RERELEECQR NHEGDEDDSH VRAQQACIEA KHDKYMADMD ELFSQVDEKR 
       160        170        180        190        200
KKRDIPDYLC GKISFELMRE PCITPSGITY DRKDIEEHLQ RVGHFDPVTR 
       210        220        230 
SPLTQEQLIP NLAMKEVIDA FISENGWVED Y

Show »

Length:231

Mass (Da):27,067

Checksum:ⁱBA7782D3C2F9E1F9

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H3BS86	H3BS86_HUMAN	E3 ubiquitin-protein ligase CHIP E3 ubiquitin-protein ligase CHIP	STUB1	213	Annotation score:
H3BUD0	H3BUD0_HUMAN	E3 ubiquitin-protein ligase CHIP E3 ubiquitin-protein ligase CHIP	STUB1	185	Annotation score:
H3BTA3	H3BTA3_HUMAN	E3 ubiquitin-protein ligase CHIP E3 ubiquitin-protein ligase CHIP	STUB1	157	Annotation score:
V9GYH3	V9GYH3_HUMAN	E3 ubiquitin-protein ligase CHIP E3 ubiquitin-protein ligase CHIP	STUB1	24	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	52	A → V in AAD33400 (PubMed:10330192).Curated	1
Sequence conflictⁱ	272	R → G in AAC18038 (PubMed:9610721).Curated	1
Sequence conflictⁱ	280	L → F in AAC18038 (PubMed:9610721).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_072348	28	E → K in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. 1 Publication	1
Natural variantⁱVAR_072349	65	N → S in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination. 1 PublicationCorresponds to variant dbSNP:rs690016544EnsemblClinVar.	1
Natural variantⁱVAR_071293	79	A → D in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777347EnsemblClinVar.	1
Natural variantⁱVAR_071294	79	A → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777346EnsemblClinVar.	1
Natural variantⁱVAR_071295	123	L → V in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777344EnsemblClinVar.	1
Natural variantⁱVAR_071296	130	N → I in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777341EnsemblClinVar.	1
Natural variantⁱVAR_072350	145	K → Q in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs146251364EnsemblClinVar.	1
Natural variantⁱVAR_071297	147	W → C in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777342EnsemblClinVar.	1
Natural variantⁱVAR_071298	165	L → F in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777340EnsemblClinVar.	1
Natural variantⁱVAR_071299	236	S → T in SCAR16. 1 Publication	1
Natural variantⁱVAR_071300	240	M → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777345EnsemblClinVar.	1
Natural variantⁱVAR_071301	246	T → M in SCAR16; inhibits ubiquitin ligase activity and autoubiquitination. 2 PublicationsCorresponds to variant dbSNP:rs587777343EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_015947	1 – 72	Missing in isoform 2. 1 PublicationAdd BLAST		72

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF039689 mRNA Translation: AAC18038.1 AF129085 mRNA Translation: AAD33400.1 AF432221 mRNA Translation: AAL99927.1 AF217968 mRNA Translation: AAG17211.1 AE006464 Genomic DNA Translation: AAK61242.1 Z92544 Genomic DNA No translation available. CH471112 Genomic DNA Translation: EAW85758.1 BC007545 mRNA Translation: AAH07545.1 BC017178 mRNA Translation: AAH17178.1 BC022788 mRNA Translation: AAH22788.1 BC063617 mRNA Translation: AAH63617.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10419.1 [Q9UNE7-1] CCDS76797.1 [Q9UNE7-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001280126.1, NM_001293197.1 [Q9UNE7-2] NP_005852.2, NM_005861.3 [Q9UNE7-1]

Genome annotation databases

Ensemblⁱ	ENST00000219548; ENSP00000219548; ENSG00000103266 [Q9UNE7-1] ENST00000564370; ENSP00000456875; ENSG00000103266 [Q9UNE7-2] ENST00000565677; ENSP00000457228; ENSG00000103266 [Q9UNE7-2]
GeneIDⁱ	10273
KEGGⁱ	hsa:10273
UCSC genome browser More...UCSCⁱ	uc002cit.4 human [Q9UNE7-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UNE7	STIP1 homology and U-box containing protein 1		MACMU		539	UniRef100_Q9UNE7
STIP1 homology and U-box containing protein 1		MANLE		250
STIP1 homology and U-box containing protein 1		COLAP		250
STIP1 homology and U-box containing protein 1		PONAB		303
STIP1 homology and U-box containing protein 1		PANTR		303
+17

Protein	Similar proteins		Species	Score	Length	Source
Q9UNE7	STIP1 homology and U-box containing protein 1		MACMU		539	UniRef90_Q9UNE7
STIP1 homology and U-box containing protein 1		MANLE		250
STIP1 homology and U-box containing protein 1		COLAP		250
STIP1 homology and U-box containing protein 1		PONAB		303
STIP1 homology and U-box containing protein 1		PANTR		303
+17

Protein	Similar proteins		Species	Score	Length	Source
Q9UNE7	STIP1 homology and U-box containing protein 1		MACMU		539	UniRef50_Q9UNE7
STIP1 homology and U-box containing protein 1		MANLE		250
STIP1 homology and U-box containing protein 1		COLAP		250
STIP1 homology and U-box containing protein 1		PONAB		303
STIP1 homology and U-box containing protein 1		PANTR		303
+22

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF039689 mRNA Translation: AAC18038.1 AF129085 mRNA Translation: AAD33400.1 AF432221 mRNA Translation: AAL99927.1 AF217968 mRNA Translation: AAG17211.1 AE006464 Genomic DNA Translation: AAK61242.1 Z92544 Genomic DNA No translation available. CH471112 Genomic DNA Translation: EAW85758.1 BC007545 mRNA Translation: AAH07545.1 BC017178 mRNA Translation: AAH17178.1 BC022788 mRNA Translation: AAH22788.1 BC063617 mRNA Translation: AAH63617.1
CCDSⁱ	CCDS10419.1 [Q9UNE7-1] CCDS76797.1 [Q9UNE7-2]
RefSeqⁱ	NP_001280126.1, NM_001293197.1 [Q9UNE7-2] NP_005852.2, NM_005861.3 [Q9UNE7-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4KBQ	X-ray	2.91	A/B	21-154	[»]
	6EFK	X-ray	1.50	A/B	23-154	[»]
	6NSV	X-ray	1.30	A/B	23-152	[»]
SMRⁱ	Q9UNE7
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115563, 422 interactors
CORUMⁱ	Q9UNE7
DIPⁱ	DIP-29752N
IntActⁱ	Q9UNE7, 165 interactors
MINTⁱ	Q9UNE7
STRINGⁱ	9606.ENSP00000219548

Protein family/group databases

MoonDBⁱ	Q9UNE7 Predicted

MoonDBⁱ

Q9UNE7 Predicted

PTM databases

iPTMnetⁱ	Q9UNE7
PhosphoSitePlusⁱ	Q9UNE7
SwissPalmⁱ	Q9UNE7

Polymorphism and mutation databases

BioMutaⁱ	STUB1
DMDMⁱ	78099173

Proteomic databases

EPDⁱ	Q9UNE7
jPOSTⁱ	Q9UNE7
MassIVEⁱ	Q9UNE7
PaxDbⁱ	Q9UNE7
PeptideAtlasⁱ	Q9UNE7
PRIDEⁱ	Q9UNE7
ProteomicsDBⁱ	85282 [Q9UNE7-1] 85283 [Q9UNE7-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	10273

DNASUⁱ

10273

Genome annotation databases

Ensemblⁱ	ENST00000219548; ENSP00000219548; ENSG00000103266 [Q9UNE7-1] ENST00000564370; ENSP00000456875; ENSG00000103266 [Q9UNE7-2] ENST00000565677; ENSP00000457228; ENSG00000103266 [Q9UNE7-2]
GeneIDⁱ	10273
KEGGⁱ	hsa:10273
UCSCⁱ	uc002cit.4 human [Q9UNE7-1]

Organism-specific databases

CTDⁱ	10273
DisGeNETⁱ	10273
GeneCardsⁱ	STUB1
HGNCⁱ	HGNC:11427 STUB1
HPAⁱ	CAB037202 CAB037209 HPA041222 HPA043531
MalaCardsⁱ	STUB1
MIMⁱ	607207 gene 615768 phenotype 618093 phenotype
neXtProtⁱ	NX_Q9UNE7
OpenTargetsⁱ	ENSG00000103266
Orphanetⁱ	412057 Autosomal recessive cerebellar ataxia due to STUB1 deficiency
PharmGKBⁱ	PA36227
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG4642 Eukaryota ENOG410ZC2R LUCA
GeneTreeⁱ	ENSGT00930000151045
HOGENOMⁱ	CLU_056455_1_0_1
InParanoidⁱ	Q9UNE7
KOⁱ	K09561
OMAⁱ	QEAATCY
OrthoDBⁱ	1422450at2759
PhylomeDBⁱ	Q9UNE7
TreeFamⁱ	TF313937

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
BRENDAⁱ	2.3.2.B10 2681
Reactomeⁱ	R-HSA-2173788 Downregulation of TGF-beta receptor signaling R-HSA-8863795 Downregulation of ERBB2 signaling R-HSA-8939902 Regulation of RUNX2 expression and activity R-HSA-8948751 Regulation of PTEN stability and activity R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkⁱ	Q9UNE7
SIGNORⁱ	Q9UNE7

Miscellaneous databases

ChiTaRSⁱ	STUB1 human
GeneWikiⁱ	STUB1
GenomeRNAiⁱ	10273
Pharosⁱ	Q9UNE7 Tbio
Protein Ontology More...PROⁱ	PR:Q9UNE7
RNActⁱ	Q9UNE7 protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000103266 Expressed in lateral nuclear group of thalamus and 226 other tissues
ExpressionAtlasⁱ	Q9UNE7 baseline and differential
Genevisibleⁱ	Q9UNE7 HS

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit 3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR041312 CHIP_TPR_N IPR013026 TPR-contain_dom IPR011990 TPR-like_helical_dom_sf IPR019734 TPR_repeat IPR003613 Ubox_domain IPR013083 Znf_RING/FYVE/PHD
Pfamⁱ	View protein in Pfam PF18391 CHIP_TPR_N, 1 hit 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
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CHIP_HUMAN
Accessionⁱ	Q9UNE7Primary (citable) accession number: Q9UNE7 Secondary accession number(s): A2IDB9 , O60526, Q969U2, Q9HBT1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
	Last sequence update:	October 25, 2005
	Last modified:	February 26, 2020
	This is version 188 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

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UniProtKB - Q9UNE7 (CHIP_HUMAN)

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E3 ubiquitin-protein ligase CHIP

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<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

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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

Protein family/group 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

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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

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Polymorphism and mutation databases

<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

Organism-specific 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

Miscellaneous 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

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ