UniProt functional annotation for Q9NXW2



	UniProt functional annotation for Q9NXW2

UniProt code: Q9NXW2.

Organism: Homo sapiens (Human).

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

Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway (PubMed:21150129, PubMed:21148293). Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities (PubMed:21148293). Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers (PubMed:27916661). While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear (PubMed:24732912). {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.

Function: (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection (PubMed:21673190, PubMed:24675744). {ECO:0000269|PubMed:21673190, ECO:0000269|PubMed:24675744}.

Subunit: Homodimer and homotetramer (PubMed:27916661). Interacts (via J domain) with HSPA8/Hsc70 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744). {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24675744, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.

Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:24732912}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to the endoplasmic reticulum membrane (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.

Ptm: Methylated at His-185 by METTL9. {ECO:0000305|PubMed:33563959}.

Similarity: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily. {ECO:0000305}.

Sequence caution: Sequence=BAB15289.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAH13619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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:		Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway (PubMed:21150129, PubMed:21148293). Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities (PubMed:21148293). Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers (PubMed:27916661). While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear (PubMed:24732912). {ECO:0000269\|PubMed:21148293, ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27916661}.



Function:		(Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection (PubMed:21673190, PubMed:24675744). {ECO:0000269\|PubMed:21673190, ECO:0000269\|PubMed:24675744}.


Subunit:		Homodimer and homotetramer (PubMed:27916661). Interacts (via J domain) with HSPA8/Hsc70 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744). {ECO:0000269\|PubMed:21148293, ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:24675744, ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27916661}.
Subcellular location:		Endoplasmic reticulum membrane {ECO:0000269\|PubMed:21148293, ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269\|PubMed:24732912}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to the endoplasmic reticulum membrane (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). {ECO:0000269\|PubMed:21148293, ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27916661}.
Ptm:		Methylated at His-185 by METTL9. {ECO:0000305\|PubMed:33563959}.
Similarity:		Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily. {ECO:0000305}.
Sequence caution:		Sequence=BAB15289.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAH13619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};