UniProt functional annotation for Q9H3M7



	UniProt functional annotation for Q9H3M7

UniProt code: Q9H3M7.

Organism: Homo sapiens (Human).

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

Function: May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1). {ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:21460850}.

Subunit: Homodimer; disulfide-linked. Interacts with TXN/thioredoxin through its redox-active site. Interacts with transcriptional repressors ZBTB16, ZBTB32 and HDAC1. Interacts (via C-terminus) with ITCH (via WW domains). Interacts with DDIT4. {ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:20068034, ECO:0000269|PubMed:21460850, ECO:0000269|PubMed:23519408}.

Subcellular location: Cytoplasm {ECO:0000250}.

Induction: By 1,25-dihydroxyvitamin D-3 and TGFB1. Down-regulated in response to oxidative stress. {ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:8086474}.

Ptm: Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH resulting in proteasomal degradation. {ECO:0000269|PubMed:20068034}.

Similarity: Belongs to the arrestin family. {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 act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1). {ECO:0000269\|PubMed:12821938, ECO:0000269\|PubMed:17603038, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:21460850}.


Subunit:		Homodimer; disulfide-linked. Interacts with TXN/thioredoxin through its redox-active site. Interacts with transcriptional repressors ZBTB16, ZBTB32 and HDAC1. Interacts (via C-terminus) with ITCH (via WW domains). Interacts with DDIT4. {ECO:0000269\|PubMed:12821938, ECO:0000269\|PubMed:17603038, ECO:0000269\|PubMed:20068034, ECO:0000269\|PubMed:21460850, ECO:0000269\|PubMed:23519408}.
Subcellular location:		Cytoplasm {ECO:0000250}.
Induction:		By 1,25-dihydroxyvitamin D-3 and TGFB1. Down-regulated in response to oxidative stress. {ECO:0000269\|PubMed:12821938, ECO:0000269\|PubMed:17603038, ECO:0000269\|PubMed:8086474}.
Ptm:		Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH resulting in proteasomal degradation. {ECO:0000269\|PubMed:20068034}.
Similarity:		Belongs to the arrestin family. {ECO:0000305}.