UniProt functional annotation for Q9UPQ7



	UniProt functional annotation for Q9UPQ7

UniProt code: Q9UPQ7.

Organism: Homo sapiens (Human).

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

Function: E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation. {ECO:0000250|UniProtKB:Q69ZS0}.

Catalytic activity: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;

Pathway: Protein modification; protein ubiquitination.

Subunit: Interacts with NLGN1 and EFNB2. Interacts with UBE2D2 and with MUSK via the first PDZ domain. {ECO:0000250}.

Subcellular location: Cell junction, synapse {ECO:0000250|UniProtKB:Q69ZS0}. Cytoplasm {ECO:0000250|UniProtKB:E7FDW2}. Note=Localizes to the postsynaptic region of neuromuscular junctions. {ECO:0000250|UniProtKB:Q69ZS0}.

Tissue specificity: Widely expressed, including in the heart, skeletal muscle and liver and, at lower levels, in the brain, colon, small intestine, placenta and lung. Down-regulated in ovarian serous papillary tumors. {ECO:0000269|PubMed:10470851, ECO:0000269|PubMed:15305371, ECO:0000269|PubMed:17118964}.

Domain: The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000250}.

Ptm: Auto-ubiquitinated. {ECO:0000250}.

Sequence caution: Sequence=BAA83047.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAC11068.1; Type=Erroneous initiation; 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:		E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation. {ECO:0000250\|UniProtKB:Q69ZS0}.


Catalytic activity:		Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
Pathway:		Protein modification; protein ubiquitination.
Subunit:		Interacts with NLGN1 and EFNB2. Interacts with UBE2D2 and with MUSK via the first PDZ domain. {ECO:0000250}.
Subcellular location:		Cell junction, synapse {ECO:0000250\|UniProtKB:Q69ZS0}. Cytoplasm {ECO:0000250\|UniProtKB:E7FDW2}. Note=Localizes to the postsynaptic region of neuromuscular junctions. {ECO:0000250\|UniProtKB:Q69ZS0}.
Tissue specificity:		Widely expressed, including in the heart, skeletal muscle and liver and, at lower levels, in the brain, colon, small intestine, placenta and lung. Down-regulated in ovarian serous papillary tumors. {ECO:0000269\|PubMed:10470851, ECO:0000269\|PubMed:15305371, ECO:0000269\|PubMed:17118964}.
Domain:		The RING-type zinc finger domain is required for E3 ligase activity. {ECO:0000250}.
Ptm:		Auto-ubiquitinated. {ECO:0000250}.
Sequence caution:		Sequence=BAA83047.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAC11068.1; Type=Erroneous initiation; Evidence={ECO:0000305};