4R3Z

Crystal structure of human ArgRS-GlnRS-AIMP1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0001525	biological_process	angiogenesis
A	0001937	biological_process	negative regulation of endothelial cell proliferation
A	0003723	molecular_function	RNA binding
A	0005125	molecular_function	cytokine activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005783	cellular_component	endoplasmic reticulum
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006915	biological_process	apoptotic process
A	0006954	biological_process	inflammatory response
A	0007165	biological_process	signal transduction
A	0007267	biological_process	cell-cell signaling
A	0009986	cellular_component	cell surface
A	0016020	cellular_component	membrane
A	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
A	0042803	molecular_function	protein homodimerization activity
A	0048514	biological_process	blood vessel morphogenesis
A	0050900	biological_process	leukocyte migration
A	0051020	molecular_function	GTPase binding
A	0051607	biological_process	defense response to virus
A	0070094	biological_process	positive regulation of glucagon secretion
B	0000049	molecular_function	tRNA binding
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004814	molecular_function	arginine-tRNA ligase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006420	biological_process	arginyl-tRNA aminoacylation
B	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
B	0034618	molecular_function	arginine binding
B	0045296	molecular_function	cadherin binding
B	0070062	cellular_component	extracellular exosome
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004819	molecular_function	glutamine-tRNA ligase activity
C	0004860	molecular_function	protein kinase inhibitor activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005759	cellular_component	mitochondrial matrix
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006425	biological_process	glutaminyl-tRNA aminoacylation
C	0007420	biological_process	brain development
C	0016874	molecular_function	ligase activity
C	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
C	0019901	molecular_function	protein kinase binding
C	0032873	biological_process	negative regulation of stress-activated MAPK cascade
C	0032991	cellular_component	protein-containing complex
C	0043039	biological_process	tRNA aminoacylation
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	2001234	biological_process	negative regulation of apoptotic signaling pathway

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PniAKeMHVGHL

Chain	Residue	Details
B	PRO201-LEU212
C	PRO270-ALA281

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Region: {"description":"Required for fibroblast proliferation"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	14
Details	Region: {"description":"Interaction with tRNA","evidences":[{"source":"UniProtKB","id":"Q05506","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Motif: {"description":"'HIGH' region"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24859084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Q2T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	10
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"26869582","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"26869582","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00962","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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