STUB1

From Wikipedia, the free encyclopedia

STIP1 homology and U-box containing protein 1

PDB rendering based on 2c2l.

Available structures: 2c2l, 2c2v

Identifiers

Symbol(s)

STUB1; CHIP; HSPABP2; NY-CO-7; SDCCAG7; UBOX1

External IDs

OMIM: 607207 MGI: 1891731 HomoloGene: 4281

Gene ontology
Molecular Function:	• ubiquitin-protein ligase activity • ligase activity • Hsp70 protein binding • protein binding, bridging • protein homodimerization activity • SMAD binding • Hsp90 protein binding
Cellular Component:	• ubiquitin ligase complex • ubiquitin conjugating enzyme complex
Biological Process:	• protein polyubiquitination • protein folding • ubiquitin-dependent SMAD protein catabolic process • proteasomal ubiquitin-dependent protein catabolic process • protein maturation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005861 (mRNA)
NP_005852 (protein)

NM_019719 (mRNA)
NP_062693 (protein)

Location

Chr 16: 0.67 - 0.67 Mb

Chr 17: 25.56 - 25.56 Mb

Pubmed search

[1]

[2]

STIP1 homology and U-box containing protein 1, also known as STUB1, is a human gene.^[1]

[edit] References

^ Entrez Gene: STUB1 STIP1 homology and U-box containing protein 1.

[edit] Further reading

Patterson C (2002). "A new gun in town: the U box is a ubiquitin ligase domain.". Sci. STKE 2002 (116): PE4. doi:10.1126/stke.2002.116.pe4. PMID 11805346.
Scanlan MJ, Chen YT, Williamson B, et al. (1998). "Characterization of human colon cancer antigens recognized by autologous antibodies.". Int. J. Cancer 76 (5): 652–8. PMID 9610721.
Ballinger CA, Connell P, Wu Y, et al. (1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.". Mol. Cell. Biol. 19 (6): 4535–45. PMID 10330192.
Connell P, Ballinger CA, Jiang J, et al. (2001). "The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.". Nat. Cell Biol. 3 (1): 93–6. doi:10.1038/35050618. PMID 11146632.
Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.". Hum. Mol. Genet. 10 (4): 339–52. PMID 11157797.
Jiang J, Ballinger CA, Wu Y, et al. (2001). "CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation.". J. Biol. Chem. 276 (46): 42938–44. doi:10.1074/jbc.M101968200. PMID 11557750.
Demand J, Alberti S, Patterson C, Höhfeld J (2002). "Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling.". Curr. Biol. 11 (20): 1569–77. PMID 11676916.
Imai Y, Soda M, Hatakeyama S, et al. (2002). "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity.". Mol. Cell 10 (1): 55–67. PMID 12150907.
Krackhardt AM, Witzens M, Harig S, et al. (2002). "Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX.". Blood 100 (6): 2123–31. doi:10.1182/blood-2002-02-0513. PMID 12200376.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Cardozo CP, Michaud C, Ost MC, et al. (2003). "C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation.". Arch. Biochem. Biophys. 410 (1): 134–40. PMID 12559985.
Zhou P, Fernandes N, Dodge IL, et al. (2003). "ErbB2 degradation mediated by the co-chaperone protein CHIP.". J. Biol. Chem. 278 (16): 13829–37. doi:10.1074/jbc.M209640200. PMID 12574167.
Shimura H, Schwartz D, Gygi SP, Kosik KS (2004). "CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival.". J. Biol. Chem. 279 (6): 4869–76. doi:10.1074/jbc.M305838200. PMID 14612456.
Li L, Xin H, Xu X, et al. (2004). "CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription.". Mol. Cell. Biol. 24 (2): 856–64. PMID 14701756.
Petrucelli L, Dickson D, Kehoe K, et al. (2004). "CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation.". Hum. Mol. Genet. 13 (7): 703–14. doi:10.1093/hmg/ddh083. PMID 14962978.
Galigniana MD, Harrell JM, Housley PR, et al. (2004). "Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation.". Brain Res. Mol. Brain Res. 123 (1-2): 27–36. doi:10.1016/j.molbrainres.2003.12.015. PMID 15046863.
He B, Bai S, Hnat AT, et al. (2004). "An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP).". J. Biol. Chem. 279 (29): 30643–53. doi:10.1074/jbc.M403117200. PMID 15107424.
Alberti S, Böhse K, Arndt V, et al. (2005). "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.". Mol. Biol. Cell 15 (9): 4003–10. doi:10.1091/mbc.E04-04-0293. PMID 15215316.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.