Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship.
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The human sulfatase catalog includes ARSI among four newly identified members.
"First, we determined the complete catalog of human sulfatases, which comprises 17 members (versus 14 in rodents) including four novel ones (ARSH, ARSI, ARSJ and ARSK)."
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Class I sulfatase activity requires conversion of the active-site cysteine to formylglycine.
"This unique modification mechanism, which is required for catalytic activity, has been highly conserved during evolution."
Molecular cloning and initial characterization of three novel human sulfatases.
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The study cloned newly identified human sulfatases and found restricted embryonic/cancer-cell expression for two.
"Interestingly, initial characterization of two of them showed that their expression pattern was mainly restricted to embryonic tissues and some cancer cell lines."
Characterization of the arylsulfatase I (ARSI) gene preferentially expressed in the human retinal pigment epithelium cell line ARPE-19.
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Tagged human ARSI was observed in the ER, cellular fraction, and medium.
"Transiently produced ARSI-FLAG was localized to the endoplasmic reticulum and was detected in the cellular fraction and the medium."
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SUMF1 coexpression enabled neutral-pH activity against an artificial arylsulfate substrate.
"When ARSI-FLAG and SUMF1-FLAG were coexpressed, the conditioned medium of the transfected cells showed arylsulfatase activity at a range of neutral pH."
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Cys93 is the SUMF1-dependent catalytic nucleophile.
"This result confirms that the active site of ARSI is Cys93 and that it is activated by SUMF1 as well as other ARSs."
Exome sequencing links corticospinal motor neuron disease to common neurodegenerative disorders.
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ARSI was among a set of putative hereditary spastic paraplegia candidate genes.
"By using whole-exome sequencing in combination with network analysis, we identified 18 previously unknown putative HSP genes and validated nearly all of these genes functionally or genetically."
A proteome-scale map of the human interactome network.
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The study generated a large systematic map of binary human protein interactions.
"Here, we describe a systematic map of ?14,000 high-quality human binary protein-protein interactions."
Arylsulfatase I is a novel lysosomal chondroitin endosulfatase regulating endochondral ossification.
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ARSI is a lysosomal chondroitin-4-sulfatase with acidic activity.
"Biochemical analyses of ARSI gain and loss of function cell lines and isolated cell-free systems revealed that ARSI is a novel chondroitin endosulfatase, specifically desulfating chondroitin-4-sulfate at pH 4.5."
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ARSI colocalizes with lysosomal markers and affects lysosome homeostasis.
"Colocalization studies suggested that ARSI is lysosomal, and lysosome homeostasis was altered in ARSI loss of function chondrocytes."
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Arsi loss increases chondrocyte-maturation markers.
"Finally, Arsi knockout in RCS chondrocytes caused increased expression of maturation genes, such as Col10a1 and Mmp13."
SUMF1 mediates the oxidation of cysteine to formylglycine, producing active arylsulfatases
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SUMF1 generates the formylglycine required for ARSI catalytic activity.
"SUMF1 mediates the oxidation of cysteine to formylglycine, producing active arylsulfatases"
UniProt entry for human ARSI (Q5FYB1)
Manual curation notes for human ARSI
Manual literature synthesis for human ARSI