UniProt functional annotation for Q9UHR4



	UniProt functional annotation for Q9UHR4

UniProt code: Q9UHR4.

Organism: Homo sapiens (Human).

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

Function: May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:22921828}.

Subunit: Interacts with RAC1. Binds to F-actin. Interacts with FASLG. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor Tir. {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:21098279, ECO:0000269|PubMed:22921828}.

Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19366662}. Note=Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.

Domain: The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity). {ECO:0000250}.

Ptm: Phosphorylated on tyrosine in response to insulin. {ECO:0000269|PubMed:17430976}.

Sequence caution: Sequence=AAD20937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=AAS07549.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAB15671.1; 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:		May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269\|PubMed:17430976, ECO:0000269\|PubMed:19366662, ECO:0000269\|PubMed:22921828}.


Subunit:		Interacts with RAC1. Binds to F-actin. Interacts with FASLG. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor Tir. {ECO:0000269\|PubMed:17430976, ECO:0000269\|PubMed:19366662, ECO:0000269\|PubMed:19807924, ECO:0000269\|PubMed:21098279, ECO:0000269\|PubMed:22921828}.
Subcellular location:		Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:19366662}. Note=Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.
Domain:		The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity). {ECO:0000250}.
Ptm:		Phosphorylated on tyrosine in response to insulin. {ECO:0000269\|PubMed:17430976}.
Sequence caution:		Sequence=AAD20937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=AAS07549.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAB15671.1; Type=Erroneous initiation; Evidence={ECO:0000305};