UniProt functional annotation for Q9NYG5



	UniProt functional annotation for Q9NYG5

UniProt code: Q9NYG5.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex. {ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:18485873}.

Pathway: Protein modification; protein ubiquitination.

Subunit: The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (PubMed:26083744, PubMed:10922056, PubMed:25043029). Interacts with the cullin domain of ANAPC2 (PubMed:11739784). Interacts with UBE2D2 (PubMed:11739784). {ECO:0000269|PubMed:10922056, ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:11573242}. Nucleus {ECO:0000269|PubMed:11573242}.

Tissue specificity: Expressed at high levels in skeletal muscle and heart; in moderate levels in brain, kidney, and liver; and at low levels in colon, thymus, spleen, small intestine, placenta, lung and peripheral blood leukocyte. {ECO:0000269|PubMed:11573242}.

Domain: The RING-type zinc finger domain coordinates an additional third zinc ion.

Ptm: Auto-ubiquitinated.

Similarity: Belongs to the RING-box family. {ECO:0000305}.

Sequence caution: Sequence=AAF36134.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex. {ECO:0000269\|PubMed:11739784, ECO:0000269\|PubMed:18485873}.


Pathway:		Protein modification; protein ubiquitination.
Subunit:		The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (PubMed:26083744, PubMed:10922056, PubMed:25043029). Interacts with the cullin domain of ANAPC2 (PubMed:11739784). Interacts with UBE2D2 (PubMed:11739784). {ECO:0000269\|PubMed:10922056, ECO:0000269\|PubMed:11739784, ECO:0000269\|PubMed:25043029, ECO:0000269\|PubMed:26083744}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:11573242}. Nucleus {ECO:0000269\|PubMed:11573242}.
Tissue specificity:		Expressed at high levels in skeletal muscle and heart; in moderate levels in brain, kidney, and liver; and at low levels in colon, thymus, spleen, small intestine, placenta, lung and peripheral blood leukocyte. {ECO:0000269\|PubMed:11573242}.
Domain:		The RING-type zinc finger domain coordinates an additional third zinc ion.
Ptm:		Auto-ubiquitinated.
Similarity:		Belongs to the RING-box family. {ECO:0000305}.
Sequence caution:		Sequence=AAF36134.1; Type=Frameshift; Evidence={ECO:0000305};