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Protein

STIP1 homology and U box-containing protein 1

Gene

Stub1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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).3 Publications

Pathwayi

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. G-protein coupled receptor binding Source: MGI
  3. heat shock protein binding Source: HGNC
  4. Hsp70 protein binding Source: HGNC
  5. Hsp90 protein binding Source: BHF-UCL
  6. kinase binding Source: MGI
  7. ligase activity Source: UniProtKB-KW
  8. misfolded protein binding Source: MGI
  9. protein binding, bridging Source: HGNC
  10. protein homodimerization activity Source: HGNC
  11. SMAD binding Source: HGNC
  12. TPR domain binding Source: HGNC
  13. ubiquitin protein ligase activity Source: MGI
  14. ubiquitin protein ligase binding Source: UniProtKB
  15. ubiquitin-protein transferase activity Source: UniProtKB
  16. ubiquitin-ubiquitin ligase activity Source: MGI

GO - Biological processi

  1. cellular response to misfolded protein Source: UniProtKB
  2. DNA repair Source: UniProtKB-KW
  3. endoplasmic reticulum unfolded protein response Source: ParkinsonsUK-UCL
  4. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
  5. negative regulation of protein binding Source: ParkinsonsUK-UCL
  6. positive regulation of chaperone-mediated protein complex assembly Source: MGI
  7. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: HGNC
  8. positive regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  9. positive regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  10. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  11. protein autoubiquitination Source: UniProtKB
  12. protein folding Source: HGNC
  13. protein K63-linked ubiquitination Source: UniProtKB
  14. protein maturation Source: HGNC
  15. protein polyubiquitination Source: HGNC
  16. protein ubiquitination Source: HGNC
  17. regulation of glucocorticoid metabolic process Source: HGNC
  18. ubiquitin-dependent protein catabolic process Source: UniProtKB
  19. ubiquitin-dependent SMAD protein catabolic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_294789. Downregulation of TGF-beta receptor signaling.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_348099. Signaling by ERBB2.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
STIP1 homology and U box-containing protein 1Curated (EC:6.3.2.-2 Publications)
Alternative name(s):
Carboxy terminus of Hsp70-interacting protein1 Publication
E3 ubiquitin-protein ligase CHIPCurated
Gene namesi
Name:Stub1Imported
Synonyms:Chip1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1891731. Stub1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus By similarity

  3. Note: Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg).By similarity

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. endoplasmic reticulum Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. intermediate filament cytoskeleton Source: MGI
  5. nuclear inclusion body Source: MGI
  6. nucleoplasm Source: MGI
  7. plasma membrane Source: MGI
  8. ubiquitin conjugating enzyme complex Source: HGNC
  9. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21K → R: Impaired interaction with ATXN3; when associated with R-4 and R-7. 1 Publication
Mutagenesisi4 – 41K → R: Impaired interaction with ATXN3; when associated with R-2 and R-7. 1 Publication
Mutagenesisi7 – 71K → R: Impaired interaction with ATXN3; when associated with R-2 and R-4. 1 Publication
Mutagenesisi261 – 2611H → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication
Mutagenesisi270 – 2701P → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304STIP1 homology and U box-containing protein 1PRO_0000106330Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki2 – 2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei20 – 201Phosphoserine2 Publications
Cross-linki23 – 23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei26 – 261Phosphoserine1 Publication
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki256 – 256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei274 – 2741PhosphoserineBy similarity

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

MaxQBiQ9WUD1.
PaxDbiQ9WUD1.
PRIDEiQ9WUD1.

PTM databases

PhosphoSiteiQ9WUD1.

Expressioni

Inductioni

Up-regulated by inflammatory signals in Treg regulatory T-cells (Treg).1 Publication

Gene expression databases

BgeeiQ9WUD1.
CleanExiMM_STUB1.
GenevestigatoriQ9WUD1.

Interactioni

Subunit structurei

Homodimer. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts (via TPR repeats) 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 the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W. Interacts with DNAJB6. Interacts with FOXP3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IlkO552227EBI-773027,EBI-6690138
UBE2NP610882EBI-773027,EBI-1052908From a different organism.

Protein-protein interaction databases

BioGridi207969. 36 interactions.
DIPiDIP-29751N.
IntActiQ9WUD1. 13 interactions.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 3913Combined sources
Helixi43 – 5614Combined sources
Helixi61 – 7313Combined sources
Helixi77 – 9014Combined sources
Helixi95 – 10713Combined sources
Helixi111 – 12717Combined sources
Helixi135 – 15218Combined sources
Helixi161 – 17818Combined sources
Turni179 – 1813Combined sources
Helixi183 – 1853Combined sources
Turni186 – 1883Combined sources
Helixi191 – 1944Combined sources
Helixi196 – 21823Combined sources
Helixi230 – 2323Combined sources
Turni235 – 2373Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi252 – 2543Combined sources
Helixi255 – 26410Combined sources
Turni270 – 2723Combined sources
Helixi278 – 2803Combined sources
Helixi285 – 29814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C2LX-ray3.30A/B/C/D24-304[»]
2C2VX-ray2.90S/T/U/V227-304[»]
3Q47X-ray1.70B23-155[»]
3Q49X-ray1.54B23-155[»]
3Q4AX-ray1.54B23-155[»]
ProteinModelPortaliQ9WUD1.
SMRiQ9WUD1. Positions 24-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WUD1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 6034TPR 1Add
BLAST
Repeati61 – 9434TPR 2Add
BLAST
Repeati96 – 12833TPR 3Add
BLAST
Domaini227 – 30175U-boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 196Poly-Gly

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

Sequence similaritiesi

Contains 3 TPR repeats.PROSITE-ProRule annotation
Contains 1 U-box domain.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiNOG260504.
GeneTreeiENSGT00730000111218.
HOGENOMiHOG000163725.
HOVERGENiHBG053046.
InParanoidiQ9WUD1.
KOiK09561.
OMAiQENELHS.
OrthoDBiEOG79W95G.
PhylomeDBiQ9WUD1.
TreeFamiTF313937.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00515. TPR_1. 1 hit.
PF04564. U-box. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
SM00504. Ubox. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
PS51698. U_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WUD1-1 [UniParc]FASTAAdd 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201S → T in BAB22329 (PubMed:16141072).Curated

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.
CCDSiCCDS28533.1.
RefSeqiNP_062693.1. NM_019719.3.
UniGeneiMm.277599.
Mm.491120.

Genome annotation databases

EnsembliENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615.
GeneIDi56424.
KEGGimmu:56424.
UCSCiuc008bcf.1. mouse.

Cross-referencesi

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.
CCDSiCCDS28533.1.
RefSeqiNP_062693.1. NM_019719.3.
UniGeneiMm.277599.
Mm.491120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C2LX-ray3.30A/B/C/D24-304[»]
2C2VX-ray2.90S/T/U/V227-304[»]
3Q47X-ray1.70B23-155[»]
3Q49X-ray1.54B23-155[»]
3Q4AX-ray1.54B23-155[»]
ProteinModelPortaliQ9WUD1.
SMRiQ9WUD1. Positions 24-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207969. 36 interactions.
DIPiDIP-29751N.
IntActiQ9WUD1. 13 interactions.

PTM databases

PhosphoSiteiQ9WUD1.

Proteomic databases

MaxQBiQ9WUD1.
PaxDbiQ9WUD1.
PRIDEiQ9WUD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615.
GeneIDi56424.
KEGGimmu:56424.
UCSCiuc008bcf.1. mouse.

Organism-specific databases

CTDi10273.
MGIiMGI:1891731. Stub1.

Phylogenomic databases

eggNOGiNOG260504.
GeneTreeiENSGT00730000111218.
HOGENOMiHOG000163725.
HOVERGENiHBG053046.
InParanoidiQ9WUD1.
KOiK09561.
OMAiQENELHS.
OrthoDBiEOG79W95G.
PhylomeDBiQ9WUD1.
TreeFamiTF313937.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_294789. Downregulation of TGF-beta receptor signaling.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_348099. Signaling by ERBB2.

Miscellaneous databases

EvolutionaryTraceiQ9WUD1.
NextBioi312582.
PROiQ9WUD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUD1.
CleanExiMM_STUB1.
GenevestigatoriQ9WUD1.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00515. TPR_1. 1 hit.
PF04564. U-box. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
SM00504. Ubox. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
PS51698. U_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Embryo and Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  4. "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF HIS-261 AND PRO-270.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
  9. "The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3."
    Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H., Li Y.
    , Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.
    Immunity 39:272-285(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FOXP3, INDUCTION.
  10. "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.

Entry informationi

Entry nameiCHIP_MOUSE
AccessioniPrimary (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: April 1, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.