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HPMR

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Ubiquitin-like 5 OKDB#: 1416
 Symbols: UBL5 Species: human
 Synonyms: HUB1,HUB1, S. CEREVISIAE, HOMOLOG OF, HUB1  Locus: 19p13.3 in Homo sapiens


For retrieval of Nucleotide and Amino Acid sequences please go to: OMIM Entrez Gene
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General Comment Ubiquitin, a small protein consisting of 76 amino acids, has been found in all eukaryotic cells studied. It is one of the most conserved proteins known; the amino acid sequence is identical from insects to humans, and there are only 3 substitutions within the plant and yeast sequences. Two classes of ubiquitin genes are recognized. Class I is a polyubiquitin gene encoding a polyprotein of tandemly repeated ubiquitins . The class II genes are fusion products between a single ubiquitin gene and 1 of 2 other possible sequences, either 52 or 76 to 80 predominantly basic amino acids. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation, which eliminates most intracellular defective problems as well as normal proteins with a rapid turnover. Degradation involves covalent binding of ubiquitin to the protein to be degraded, through isopeptide bonds from the C-terminal glycine residue to the epsilon-amino groups of lysyl side chains.

NCBI Summary: Ubiquitin-like proteins (UBLs) are thought to be reversible modulators of protein function rather than protein degraders like ubiquitin (MIM 191339).[supplied by OMIM]
General function Cell cycle regulation
Comment
Cellular localization Cytoplasmic
Comment
Ovarian function
Comment
Expression regulated by
Comment
Ovarian localization Oocyte
Comment Sutovsky et al. (1999) demonstrated that sperm mitochondria are selectively marked for destruction by a ubiquitin tag. In fertilized eggs from rhesus monkeys and cows the ubiquitination was evident at first mitosis. Participation of the ubiquitin-proteasome pathway in rat oocyte activation Tan X, et al . The role of the ubiquitin-proteasome pathway (UPP) in mitosis is well known. However, its role in meiotic division is still poorly documented, especially in the activation of mammalian oocytes. In this study, the role of proteasome in the spontaneous and parthenogenetic activation of rat oocytes was investigated. We found that ALLN, an inhibitor of proteasome, when applied to metaphase II oocytes, inhibited spontaneous activation, blocked extrusion of the second polar body (PB) and caused the withdrawal of the partially extruded second PB. ALLN also inhibited the parthenogenetic activation induced by cycloheximide, but had no effect on the formation of pronuclei in activated eggs. In metaphase and anaphase, ubiquitin and proteasome localized to the meiotic spindle, concentrating on both sides of the oocyte-second PB boundary during PB extrusion. This pattern of cellular distribution suggests that UPP may have a role in regulating nuclear division and cytokinesis. Ubiquitin was seen to form a ring around the pronucleus, whereas proteasome was evenly distributed in the pronuclear region. Taken together, our results indicate that (1) UPP is required for the transitions of oocytes from metaphase II to anaphase II and from anaphase II to the end of meiosis; and (2) the UPP plays a role in cytokinesis of the second meiotic division.
Follicle stages
Comment
Phenotypes
Mutations 0 mutations
Genomic Region show genomic region
Phenotypes and GWAS show phenotypes and GWAS
Links
OMIM (Online Mendelian Inheritance in Man: an excellent source of general gene description and genetic information.)
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created: Jan. 17, 2002, 4:06 p.m. by: hsueh   email:
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last update: July 7, 2005, 12:39 a.m. by: system    email:



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