Tässä mainitaan E3 ubikitiiniligaasi. Otan siitä tietoja. Sitä mainitaan eäiten syöpien yhteydessä (Pirh2 nimellä) .Sars koronavirusyhteydessä sitä maintian RCHY1 nimellä, joka korostaa sen sinkkisormirakennetta. Minä taas tunnen sen vihkoni systemaattisista RNF proteiineista nimellä RNF199. Tässä tuli varmistettua , että minulla on se jo tallessa.
RCHY1 (ring finger and CHY zinc finger domain containing 1)
- Also known as ZCHY; ARNIP; CHIMP; PIRH2; RNF199; ZNF363; PRO1996
- Summary. The protein encoded by this gene has ubiquitin ligase activity. It mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including tumor protein 53, histone deacetylase 1, and cyclin-dependent kinase inhibitor 1B, thus regulating their levels and cell cycle progression. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Jun 2013]
- Expression: Ubiquitous expression in thyroid (RPKM 7.9), bone marrow (RPKM 6.3) and 25 other tissues See more
- Orthologs mouse all
- Preferred Names
- RING finger and CHY zinc finger domain-containing protein 1
- Names
- CH-rich interacting match with PLAG1
- E3 ubiquitin-protein ligase Pirh2
- RING finger protein 199
- RING-type E3 ubiquitin transferase RCHY1
- androgen-receptor N-terminal-interacting protein
- p53-induced protein with a RING-H2 domain
- ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase
- zinc finger protein 363
- zinc finger, CHY-type
- STRUKTUURISTA:
- Conserved Domains (3) summary
-
- pfam05495
Location:20 → 91 - zf-CHY; CHY zinc finger
- pfam14599
Location:182 → 240 - zinc_ribbon_6; Zinc-ribbon
- cl17238
Location:144 → 178 - RING_Ubox; The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain
- pfam05495
- YKSITYISKOHTIA RAKENTEESTA
FEATURES Location/Qualifiers source 1..252 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="4" /map="4q21.1" Protein 1..252 /product="RING finger and CHY zinc finger domain-containing protein 1 isoform 3" /EC_number="2.3.2.27" /note="zinc finger protein 363; androgen-receptor N-terminal-interacting protein; ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase; CH-rich interacting match with PLAG1; RING finger protein 199; E3 ubiquitin-protein ligase Pirh2; p53-induced protein with a RING-H2 domain; zinc finger, CHY-type; RING-type E3 ubiquitin transferase RCHY1" /calculated_mol_wt=28852 Region 20..91 /region_name="zf-CHY" /note="CHY zinc finger; pfam05495" /db_xref="CDD:310238" Region 144..178 /region_name="RING_Ubox" /note="The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; cl17238" /db_xref="CDD:327409" Site order(145,148,164,166,169,174,177) /site_type="other" /note="cross-brace motif" /db_xref="CDD:319361" Region 182..240 /region_name="zinc_ribbon_6" /note="Zinc-ribbon; pfam14599" /db_xref="CDD:317052" CDS 1..252 /gene="RCHY1" /gene_synonym="ARNIP; CHIMP; PIRH2; PRO1996; RNF199; ZCHY; ZNF363" /coded_by="NM_001009922.2:145..903" /note="isoform 3 is encoded by transcript variant 3" /db_xref="CCDS:CCDS34012.1" /db_xref="GeneID:25898" /db_xref="HGNC:HGNC:17479" /db_xref="MIM:607680" ORIGIN 1 maataredga sgqergqrgc ehydrgcllk apccdklytc rlchdnnedh qldrfkvkev 61 qcincekiqh aqqtceecst lfgeyycdic hlfdkdkkqy hcencgicri gpkedffhcl 121 kcnlclamnl qgrhkcienv srqncpicle dihtsrvvah vlpcghllhr gyrcplcmhs 181 aldmtrywrq lddevaqtpm pseyqnmtvd ilcndcngrs tvqfhilgmk ckicesynta 241 qaggrrisld qq
- Muutamia referfenssejä :
REFERENCE 7 (residues 1 to 252)
AUTHORS Corcoran CA, Huang Y and Sheikh MS.
TITLE The p53 paddy wagon: COP1, Pirh2 and MDM2 are found resisting
apoptosis and growth arrest
JOURNAL Cancer Biol. Ther. 3 (8), 721-725 (2004)
REFERENCE 8 (residues 1 to 252)
AUTHORS Logan IR, Sapountzi V, Gaughan L, Neal DE and Robson CN.
TITLE Control of human PIRH2 protein stability: involvement of TIP60 and
the proteosome
JOURNAL J. Biol. Chem. 279 (12), 11696-11704 (2004)
PUBMED 14701804
TITLE Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53
degradation
JOURNAL Cell 112 (6), 779-791 (2003)
PUBMED 12654245
- Measles virus: evidence for association with lung cancer. Sion-Vardy N, et al. Exp Lung Res, 2009 Oct. PMID 19895323
- Data indicate cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication.
- Overexpression of Pirh2 decreased the replication of prototype foamy virus, whereas knockdown of Pirh2 with specific siRNA increased PFV replication.
- https://www.ncbi.nlm.nih.gov/pubmed/19043414
Abstract Pirh2 (p53-induced RING-H2 domain protein; also known as Rchy1) is an E3 ubiquitin ligase involved in a negative-feedback loop with p53. Using NMR spectroscopy, we show that Pirh2 is a unique cysteine-rich protein comprising three modular domains. The protein binds nine zinc ions using a variety of zinc coordination schemes, including a RING domain and a left-handed beta-spiral in which three zinc ions align three consecutive small beta-sheets in an interleaved fashion. We show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. As a result, Pirh2 preferentially ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting that Pirh2 regulates protein turnover of the transcriptionally active form of p53.
- PMID:
- 19043414
- PMCID:
- PMC4075976
- DOI:
- 10.1038/nsmb.1521
- [Indexed for MEDLINE]
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4075976/figure/F2/
- SARS Coronavirus noteeraa tämän E3- ubikitiiniligaasin.
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