glyS protein (Pseudomonas aeruginosa) - STRING interaction network

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gene neighborhood

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textmining

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Score

glyS

glyS- glycine--tRNA ligase, beta subunit (684 aa)

Predicted Functional Partners:

glyQ

0.999

ileS

0.823

aspS

0.812

cysS

0.764

proS

0.745

pheT

0.733

ribD

0.733

tag

0.721

rpsF

0.709

glnS

0.705

Your Current Organism:

Pseudomonas aeruginosa

NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
aspS	cysS	DR97_974	DR97_91	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	0.839
aspS	glnS	DR97_974	DR97_92	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	glnS- glutamine--tRNA ligase	0.720
aspS	glyQ	DR97_974	DR97_2962	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	glyQ- glycine--tRNA ligase, alpha subunit	0.637
aspS	glyS	DR97_974	DR97_2961	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	glyS- glycine--tRNA ligase, beta subunit	0.812
aspS	ileS	DR97_974	DR97_1864	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile)	0.873
aspS	pheT	DR97_974	DR97_5223	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	pheT_bact- phenylalanine--tRNA ligase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily	0.765
aspS	proS	DR97_974	DR97_981	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	Proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction- proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as ’pretransfer’ editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated ’posttransfer’ editing and involves deacy [...]	0.781
aspS	ribD	DR97_974	DR97_3811	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family	0.544
cysS	aspS	DR97_91	DR97_974	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	0.839
cysS	glnS	DR97_91	DR97_92	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	glnS- glutamine--tRNA ligase	0.983
cysS	glyQ	DR97_91	DR97_2962	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	glyQ- glycine--tRNA ligase, alpha subunit	0.731
cysS	glyS	DR97_91	DR97_2961	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	glyS- glycine--tRNA ligase, beta subunit	0.764
cysS	ileS	DR97_91	DR97_1864	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile)	0.941
cysS	pheT	DR97_91	DR97_5223	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	pheT_bact- phenylalanine--tRNA ligase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily	0.846
cysS	proS	DR97_91	DR97_981	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	Proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction- proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as ’pretransfer’ editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated ’posttransfer’ editing and involves deacy [...]	0.850
cysS	ribD	DR97_91	DR97_3811	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family	0.590
cysS	rpsF	DR97_91	DR97_2286	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA	0.434
glnS	aspS	DR97_92	DR97_974	glnS- glutamine--tRNA ligase	Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily	0.720
glnS	cysS	DR97_92	DR97_91	glnS- glutamine--tRNA ligase	cysS- cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family	0.983
glnS	glyQ	DR97_92	DR97_2962	glnS- glutamine--tRNA ligase	glyQ- glycine--tRNA ligase, alpha subunit	0.705

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