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1DG3

STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001530molecular_functionlipopolysaccharide binding
A0003779molecular_functionactin binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0004382molecular_functionGDP phosphatase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0012506cellular_componentvesicle membrane
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0019899molecular_functionenzyme binding
A0019955molecular_functioncytokine binding
A0030507molecular_functionspectrin binding
A0030659cellular_componentcytoplasmic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0032703biological_processnegative regulation of interleukin-2 production
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042832biological_processdefense response to protozoan
A0045087biological_processinnate immune response
A0050848biological_processregulation of calcium-mediated signaling
A0050860biological_processnegative regulation of T cell receptor signaling pathway
A0051607biological_processdefense response to virus
A0051715biological_processcytolysis in another organism
A0051879molecular_functionHsp90 protein binding
A0070373biological_processnegative regulation of ERK1 and ERK2 cascade
A0071346biological_processcellular response to type II interferon
A0071347biological_processcellular response to interleukin-1
A0071356biological_processcellular response to tumor necrosis factor
A0072665biological_processprotein localization to vacuole
A0106139cellular_componentsymbiont cell surface
A0140639biological_processpositive regulation of pyroptotic inflammatory response
A0160075biological_processnon-canonical inflammasome complex assembly
A1900025biological_processnegative regulation of substrate adhesion-dependent cell spreading
A1903076biological_processregulation of protein localization to plasma membrane
A1903077biological_processnegative regulation of protein localization to plasma membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10676968, ECO:0000269|PubMed:10970849, ECO:0000269|PubMed:16511497, ECO:0007744|PDB:1F5N, ECO:0007744|PDB:2B8W, ECO:0007744|PDB:2B92, ECO:0007744|PDB:2D4H
ChainResidueDetails
AGLY45
ALEU67

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10676968, ECO:0000269|PubMed:10970849, ECO:0007744|PDB:1F5N
ChainResidueDetails
AASP97

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PIM1 => ECO:0000269|PubMed:37797010
ChainResidueDetails
ASER156

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000305|PubMed:8830800
ChainResidueDetails
ACYS589

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PIM1 => ECO:0000269|PubMed:37797010
ChainResidueDetails
ATHR590

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:31268602, ECO:0000269|PubMed:32510692, ECO:0000269|PubMed:8830800
ChainResidueDetails
ACYS589

site_idSWS_FT_FI7
Number of Residues9
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:29144452
ChainResidueDetails
ALYS207
ALYS209
ALYS210
ALYS382
ALYS562
ALYS567
ALYS573
ALYS587

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PDB entries from 2024-10-30

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