UniProt functional annotation for P10586



	UniProt functional annotation for P10586

UniProt code: P10586.

Organism: Homo sapiens (Human).

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

Function: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.

Function: The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.

Catalytic activity: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- ProRule:PRU10044};

Subunit: Interacts with GRIP1 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR. {ECO:0000250, ECO:0000269|PubMed:8995282, ECO:0000269|PubMed:9624153}.

Subcellular location: Membrane; Single-pass type I membrane protein.

Disease: Aplasia or hypoplasia of the breasts and/or nipples 2 (BNAH2) [MIM:616001]: A group of congenital deformities encompassing total absence of breasts and nipple (amastia), absence of the nipple (athelia), and absence of the mammary gland (amazia). {ECO:0000269|PubMed:24781087}. Note=The disease is caused by variants affecting the gene represented in this entry.

Similarity: Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. {ECO:0000305}.

Sequence caution: Sequence=BAD66835.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=CAA68754.1; 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:		Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.



Function:		The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.


Catalytic activity:		Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255\|PROSITE- ProRule:PRU10044};
Subunit:		Interacts with GRIP1 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR. {ECO:0000250, ECO:0000269\|PubMed:8995282, ECO:0000269\|PubMed:9624153}.
Subcellular location:		Membrane; Single-pass type I membrane protein.
Disease:		Aplasia or hypoplasia of the breasts and/or nipples 2 (BNAH2) [MIM:616001]: A group of congenital deformities encompassing total absence of breasts and nipple (amastia), absence of the nipple (athelia), and absence of the mammary gland (amazia). {ECO:0000269\|PubMed:24781087}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. {ECO:0000305}.
Sequence caution:		Sequence=BAD66835.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=CAA68754.1; Type=Erroneous initiation; Evidence={ECO:0000305};