(Q22676731)

English

Thiosulfate sulfurtransferase

mammalian protein found in Homo sapiens

thiosulfate sulfurtransferase (rhodanese)
epididymis secretory sperm binding protein
TST
Rhodanese
thiosulfate sulfurtransferase

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No description defined

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Statements

1 reference

13 November 2019

1 reference

1 December 2016

Rhodanese-like domain superfamily

1 reference

stated in

InterPro Release 71.0

reference URL

http://www.ebi.ac.uk/interpro/protein/Q16762

Rhodanese-like domain, protein family

1 reference

based on heuristic

inferred from protein domain or family

Thiosulphate sulfurtransferase, conserved site, protein family

1 reference

based on heuristic

inferred from protein domain or family

1 reference

13 November 2019

1 reference

13 November 2019

1 reference

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

IEA

thiosulfate sulfurtransferase activity

4 references

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

8 April 2019

Cloning and expression of human liver rhodanese cDNA

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

1 reference

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

IEA

cell component

mitochondrial inner membrane

1 reference

26 September 2017

Ensembl genome database project

reference URL

http://www.ebi.ac.uk/QuickGO/annotations?protein=Q16762&geneProductId=UniProtKB:Q16762

determination method

IEA

extracellular exosome

1 reference

26 September 2017

Proteomic analysis of podocyte exosome-enriched fraction from normal human urine

http://www.ebi.ac.uk/QuickGO/annotations?protein=Q16762&geneProductId=UniProtKB:Q16762

1 reference

26 September 2017

Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy

http://www.ebi.ac.uk/QuickGO/annotations?protein=Q16762&geneProductId=UniProtKB:Q16762

1 reference

8 April 2019

Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

3 references

1 reference

8 April 2019

Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

IDA

rRNA import into mitochondrion

1 reference

8 April 2019

Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import into human mitochondria

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

IMP

epithelial cell differentiation

1 reference

8 April 2019

Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco-2

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

IDA

cyanate catabolic process

1 reference

8 April 2019

Cloning and expression of human liver rhodanese cDNA

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

TAS

sulfur amino acid catabolic process

1 reference

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q16762

determination method

TAS

has part(s)

Thiosulphate sulfurtransferase, conserved site

1 reference

stated in

InterPro Release 71.0

reference URL

http://www.ebi.ac.uk/interpro/protein/Q16762

Rhodanese-like domain

1 reference

stated in

InterPro Release 71.0

reference URL

http://www.ebi.ac.uk/interpro/protein/Q16762

Identifiers

1 reference

30 May 2020

1 reference

30 May 2020

1 reference

13 November 2019

1 reference

1 reference

1 reference

1 reference

(Q22676731)

Thiosulfate sulfurtransferase

Statements

Identifiers

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