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Protein

Green fluorescent protein

Gene

GFP

Organism
Aequorea victoria (Jellyfish)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca2+-activated photoprotein aequorin.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Absorptioni

Abs(max)=395 nmExhibits a smaller absorbance peak at 470 nm. The fluorescence emission spectrum peaks at 507-510 nm with a shoulder at 545 nm (PubMed:8137953, PubMed:9154981). The exact value of the emission maximum depends on the environment of the chromophore (PubMed:10220315). As a consequence, mutant versions have been designed that have substantially shifted emission spectra, including yellow-emission variants (YFP), blue and cerulean fluorescing proteins (PubMed:9145105, PubMed:9782051, PubMed:17685554).6 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

  • bioluminescence Source: UniProtKB
  • generation of precursor metabolites and energy Source: UniProtKB
  • protein-chromophore linkage Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPhotoprotein
Biological processLuminescence
LigandChromophore

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-20291

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Green fluorescent protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GFP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAequorea victoria (Jellyfish)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6100 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaCnidariaHydrozoaHydroidolinaLeptothecataAequoreidaeAequorea

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Green fluorescent protein has been engineered to produce a vast number of variously colored mutants, fusion proteins, and biosensors. Green fluorescent protein can be mutated to emit at different wavelengths such as blue for BFP (when Tyr-66 is replaced by His), cyan for CFP (when Tyr-66 is replaced by Trp), and yellow for YFP (when THR-203 is replaced by Tyr). Further generation of mutants led to more stable proteins (at 37 degrees Celsius for example) with brighter fluorescence and longer fluorescence lifetimes. Fluorescent proteins and their mutated allelic forms have become a useful and ubiquitous tool for making chimeric proteins, where they function as a fluorescent protein tag. Typically they tolerate N- and C-terminal fusion to a broad variety of proteins. They have been expressed in most known cell types and are used as a noninvasive fluorescent marker in living cells and organisms. They enable a wide range of applications where they have functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions.8 Publications
Can also be used as a molecular thermometer, allowing accurate temperature measurements in fluids. The measurement process relies on the detection of the blinking of GFP using fluorescence correlation spectroscopy.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi30S → R in mut1.28; shifts fluorescence lifetime from 3.03 to 2.76 ns; when associated with H-145. In mut2.2; shifts fluorescence lifetime from 3.03 to 1.94 ns; when associated with H-69 and H-145. In mut3.3; shifts fluorescence lifetime from 3.03 to 1.88 ns; when associated with L-46; H-69 and H-145. In EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with N-39; H-66; A-72; T-105; F-145; V-171; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with N-39; H-66; A-72; T-105; V-128; F-145; I-150; V-155; V-171; S-198; V-206 and V-224. 2 Publications1
Mutagenesisi39Y → N in EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; H-66; A-72; T-105; F-145; V-171; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; H-66; A-72; T-105; V-128; F-145; I-150; V-155; V-171; S-198; V-206 and V-224. 1 Publication1
Mutagenesisi46F → L in mut3.3; shifts fluorescence lifetime from 3.03 to 1.88 ns; when associated with R-30; H-69 and H-145. In R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-64; N-68; Q-162; A-163; V-167 and L-171. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-64; G-65; L-68; A-72; T-153; A-163; G-175 and Y-203. 3 Publications1
Mutagenesisi64F → L in EGFP; increases fluoresence at warmer temperatures such as 37 degrees Celsius; when associated with T-65. In EBFP; gives rise to variants with blue fluorescence; when associated with T-65 and H-66. In ECFP; leads to cyan fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with T-65; W-66; I-146; T-153 and A-163. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighterH than ECFP; when associated with T-65; W-66; A-72; A-145; I-146; D-148; T-153 and A-163. In R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-46; N-68; Q-162; A-163; V-167 and L-171. In GFPmut 1; red-shifts by about 100 nm the excitation maxima, permitting efficient excitation at 488 nm and increases fluorescence; when associated with T-65. In VisGreen; leads to brighter fluorescence; when associated with T-65; A-72; K-149 and T-167. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; G-65; L-68; A-72; T-153; A-163; G-175 and Y-203. 10 Publications1
Mutagenesisi64F → M in RSGFP4; increases fluorescence and shifts the major exitation peak to 489-490 nm; when associated with G-65 and L-69. 1 Publication1
Mutagenesisi65 – 66SY → TW: Gives rise to variants with cerulean fluorsecence. 1 Publication2
Mutagenesisi65S → A in GFPmut 2; red-shifts by about 100 nm the excitation maxima, permitting efficient excitation at 488 nm and increases fluorescence; when associated with L-68 and A-72. 1 Publication1
Mutagenesisi65S → G in EYFP; leads to yellow fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with L-68; A-72 and Y-203. In GFPmut 3; highly fluorescent mutant when excited at 488 nm; when associated with A-72. Highly fluorescent; when associated with Y-203; L-68 and A-72. In RSGFP4; increases fluoresence and shifts the major exitation peak to 489-490 nm; when associated with M-64 and L-69. In YFP 10C; shifts the major emission and exitation peak up to 20 nm; when associated with L-68; A-72 and Y-203. In Topaz; shifts the major emission and exitation peak up to 20 nm; when associated with A-72; R-79 and Y-203. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; L-68; A-72; T-153; A-163; G-175 and Y-203. 6 Publications1
Mutagenesisi65S → T: Increases fluoresence, photostability and shifts the major exitation peak to 488 nm. In EGFP; increases fluoresence at warmer temperatures such as 37 degrees Celsius; when associated with L-64. In EBFP; gives rise to variants with blue fluorescence; when associated with L-64 and H-66. In GFPmut 1; red-shifts by about 100 nm the excitation maxima, permitting efficient excitation at 488 nm and increases fluorescence; when associated with T-65. In ECFP; leads to cyan fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with L-64; W-66; I-146; T-153 and A-163. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; W-66; A-72; A-145; I-146; D-148; T-153 and A-163. In Esmerald; leads to brighter fluorescence; when associated with A-72; K-149; T-153 and T-167. In VisGreen; leads to brighter fluorescence; when associated with L-64; A-72; K-149 and T-167. 8 Publications1
Mutagenesisi66Y → H in BFP; shifts the excitation and emission spectra to shorter wavelengths. In EBFP; gives rise to variants with blue fluorescence; when associated with L-64 and T-65. In Azurite; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-80; F-145; I-150 and R-224. In EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; A-72; T-105; F-145; V-171; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; A-72; T-105; V-128; F-145; I-150; V-155; V-171; S-198; V-206 and V-224. 4 Publications1
Mutagenesisi66Y → T or F: Shifts the excitation and emission spectra to shorter wavelengths. 1 Publication1
Mutagenesisi66Y → W in W; leads to excitation and emission wavelengths intermediate between tyrosine and histidine but is only weakly fluorescent. In ECFP; leads to cyan fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with L-64; T-65; I-146; T-153 and A-163. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; A-72; A-145; I-146; D-148; T-153 and A-163. 4 Publications1
Mutagenesisi68V → L in EYFP; leads to yellow fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with G-65; A-72 and Y-203. In GFPmut 2; red-shifts by about 100 nm the excitation maxima, permitting efficient excitation at 488 nm and increases fluorescence; when associated with A-65 and A-72. In Citrinine; leads to excitation and emission peaks of 516 and 529 nm, respectively; when associated with M-69; A-72 and Y-203. In YFP 10C; shifts the major emission and exitation peak up to 20 nm; when associated with G-65; A-72 and Y-203. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; G-65; A-72; T-153; A-163; G-175 and Y-203. 6 Publications1
Mutagenesisi68V → N in R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-46; L-64; Q-162; A-163; V-167 and L-171. 1 Publication1
Mutagenesisi69Q → H in P4; leads to no detectable fluorescence. In mut2.2; shifts fluorescence lifetime from 3.03 to 1.94 ns; when associated with R-30 and H-145. In mut3.3; shifts fluorescence lifetime from 3.03 to 1.88 ns; when associated with R-30; L-46 and H-145. 2 Publications1
Mutagenesisi69Q → L in RSGFP4; increases fluorescence and shifts the major exitation peak to 489-490 nm; when associated with M-64 and G-65. 1 Publication1
Mutagenesisi69Q → M in Citrinine; leads to excitation and emission peaks of 516 and 529 nm, respectively; when associated with L-68; A-72 and Y-203. 1 Publication1
Mutagenesisi72S → A: Increases fluoresence at warmer temperatures such as 37 degrees Celsius. In GFPmut 3; highly fluorescent mutant when excited at 488 nm; when associated with G-65. In EYFP; leads to yellow fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with G-65; L-68 and Y-203. In GFPmut 2; red-shifts by about 100 nm the excitation maxima, permitting efficient excitation at 488 nm and increases fluorescence; when associated with A-65 and L-68. In Citrinine; leads to excitation and emission peaks of 516 and 529 nm, respectively; when associated with L-68; M-69 and Y-203. In YFP 10C; shifts the major emission and exitation peak up to 20 nm; when associated with G-65; L-68; and Y-203. In Topaz; shifts the major emission and exitation peak up to 20 nm; when associated with G-65; R-79 and Y-203. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; W-66; A-145; I-146; D-148; T-153 and A-163. In Sapphire/H9-40; exhibits a huge Stoke's shift, with an excitation peak at 399 nm and an emission peak at 511 nm; when associated with F-145 and I-203. In EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; T-105; F-145; V-171; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; T-105; V-128; F-145; I-150; V-155; V-171; S-198; V-206 and V-224. In Esmerald; leads to brighter fluorescence; when associated with T-65; K-149; T-153 and T-167. In VisGreen; leads to brighter fluorescence; when associated with L-64; T-65; K-149 and T-167. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; G-65; L-68; T-153; A-163; G-175 and Y-203. 11 Publications1
Mutagenesisi79K → R in Topaz; shifts the major emission and exitation peak up to 20 nm; when associated with G-65; A-72 and Y-203. 1 Publication1
Mutagenesisi80Q → R in Azurite; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with H-66; F-145; I-150 and R-224. 1 Publication1
Mutagenesisi99F → S in alphaGFP/cycle 3 GFP; improves folding at 37 degrees Celsius, reduces aggregation at high concentrations, and increases the diffusibility of the protein inside cells; when associated with T-153 and A-163. 3 Publications1
Mutagenesisi103D → E in mut1.27; shifts fluorescence lifetime from 3.03 to 2.85 ns; when associated with H-145. 1 Publication1
Mutagenesisi105N → T in EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; F-145; V-171; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; V-128; F-145; I-150; V-155; V-171; S-198; V-206 and V-224. 1 Publication1
Mutagenesisi128I → V in EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; F-145; I-150; V-155; V-171; S-198; V-206 and V-224. 1 Publication1
Mutagenesisi145Y → A in Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; W-66; A-72; I-146; D-148; T-153 and A-163. 1 Publication1
Mutagenesisi145Y → C in mut1.9; shifts fluorescence lifetime from 3.03 to 2.74 ns. 1 Publication1
Mutagenesisi145Y → F in Sapphire/H9-40; exhibits a huge Stoke's shift, with an excitation peak at 399 nm and an emission peak at 511 nm; when associated with A-72 and I-203. In Azurite; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with H-66; R-80; I-150 and R-224. In EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-171; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; I-150; V-155; V-171; S-198; V-206 and V-224. 2 Publications1
Mutagenesisi145Y → H in mut1.3; shifts fluorescence lifetime from 3.03 to 2.78 ns. In mut1.5; shifts fluorescence lifetime from 3.03 to 2.72 ns; when associated with A-193. In mut1.27; shifts fluorescence lifetime from 3.03 to 2.85 ns; when associated with E-103. In mut1.28; shifts fluorescence lifetime from 3.03 to 2.76 ns; when associated with R-30. In mut2.1; shifts fluorescence lifetime from 3.03 to 2.50 ns; when associated with A-176 and I-198. In mut2.2; shifts fluorescence lifetime from 3.03 to 1.94 ns; when associated with R-30 and H-69. In mut3.3; shifts fluorescence lifetime from 3.03 to 1.88 ns; when associated with R-30; L-46 and H-69. 1 Publication1
Mutagenesisi146N → I in ECFP; leads to cyan fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with L-64; T-65; W-66; T-153 and A-163. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; W-66; A-72; A-145; D-148; T-153 and A-163. 3 Publications1
Mutagenesisi147S → P: Increases fluorescence at warmer temperatures such as 37 degrees Celsius. 1 Publication1
Mutagenesisi148H → D in Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; W-66; A-72; A-145; I-146; T-153 and A-163. 1 Publication1
Mutagenesisi149N → K: Increases fluorescence at warmer temperatures such as 37 degrees Celsius. In Esmerald; leads to brighter fluorescence; when associated with T-65; A-72; T-153 and T-167. In VisGreen; leads to brighter fluorescence; when associated with L-64; T-65; A-72 and T-167. 2 Publications1
Mutagenesisi150V → I in Azurite; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with H-66; R-80; F-145 and R-224. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; F-145; V-155; V-171; S-198; V-206 and V-224. 1 Publication1
Mutagenesisi153M → T: Increases fluorescence at warmer temperatures such as 37 degrees Celsius. In alphaGFP/cycle 3 GFP; improves folding at 37 degrees Celsius, reduces aggregation at high concentrations, and increases the diffusibility of the protein inside cells; when associated with S-99 and A-163. In ECFP; leads to cyan fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with L-64; T-65; W-66; I-146 and A-163. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; W-66; A-72; A-145; I-146; D-148 and A-163. In Esmerald; leads to brighter fluorescence; when associated with T-65; A-72; K-149 and T-167. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; G-65; L-68; A-72; A-163; G-175 and Y-203. 9 Publications1
Mutagenesisi155D → V in EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; F-145; I-150; V-171; S-198; V-206 and V-224. 1 Publication1
Mutagenesisi162K → Q in R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-46; L-64; N-68; A-163; V-167 and L-171. 1 Publication1
Mutagenesisi163V → A in GFPB; leads to enhanced fluorescence at 37 degrees Celsius. In GFPA; leads to even higher fluorescence at 37 degrees Celsius than GFPA; whenassociated with G-175. In alphaGFP/cycle 3 GFP; improves folding at 37 degrees Celsius, reduces aggregation at high concentrations, and increases the diffusibility of the protein inside cells; when associated with S-99 and T-153. In R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-46; L-64; N-68; Q-162; V-167 and L-171. In ECFP; leads to cyan fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with L-64; T-65; W-66; I-146 and T-153. In Cerulean; leads to improved quantum yield, a higher extinction coefficient and is 2.5-fold brighter than ECFP; when associated with L-64; T-65; W-66; A-72; A-145; I-146; D-148 and T-153. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; G-65; L-68; A-72; T-153; G-175 and Y-203. 9 Publications1
Mutagenesisi167I → T in P11; increases fluorescence at 475 nm excitation and at warmer temperatures such as 37 degrees Celsius. In Esmerald; leads to brighter fluorescence; when associated with T-65; A-72; K-149 and T-153. In VisGreen; leads to brighter fluorescence; when associated with L-64; T-65; A-72 and K-149. 3 Publications1
Mutagenesisi167I → V in P9; increases fluorescence at 475 nm excitation. In R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-46; L-64; N-68; Q-162; A-163 and L-171. 2 Publications1
Mutagenesisi171I → L in R10-3; matures to the red-emitting state with excitation and emission maxima at 555 and 585 nm, respectively; when associated with L-46; L-64; N-68; Q-162; A-163 and V-167. 1 Publication1
Mutagenesisi171I → V in EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; F-145; S-198 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; F-145; I-150; V-155; S-198; V-206 and V-224. 1 Publication1
Mutagenesisi175S → G in GFPA; leads to enhanced fluorescence at 37 degrees Celsius; when associated with A-163. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; G-65; L-68; A-72; T-153; A-163 and Y-203. 2 Publications1
Mutagenesisi176V → A in mut2.1; shifts fluorescence lifetime from 3.03 to 2.50 ns; when associated with H-145 and I-198. 1 Publication1
Mutagenesisi193V → A in mut1.5; shifts fluorescence lifetime from 3.03 to 2.72 ns; when associated with H-145. 1 Publication1
Mutagenesisi198N → I in mut2.1; shifts fluorescence lifetime from 3.03 to 2.50 ns; when associated with H-145 and A-176. 1 Publication1
Mutagenesisi198N → S in EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; F-145; V-171 and V-206. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; F-145; I-150; V-155; V-171; S-198 and V-224. 1 Publication1
Mutagenesisi202S → F in H9; increases fluorescence at 395 nm excitation; when associated with I-203. 1 Publication1
Mutagenesisi203T → H, W or F: Results in significantly red-shifted excitation and emission maxima. 1 Publication1
Mutagenesisi203T → I: Suppresses the 475 nm excitation peak, leaving only the shorter wavelength peak at 399 nm. In H9; increases fluorescence at 395 nm excitation; when associated with I-203. In Sapphire/H9-40; exhibits a huge Stoke's shift, with an excitation peak at 399 nm and an emission peak at 511 nm; when associated with A-72 and F-145. 3 Publications1
Mutagenesisi203T → Y: Gives rise to yellow-emission variants. In EYFP; leads to yellow fluorescence, folds faster and more efficiently at 37 degrees Celsius and has superior solubility and brightness; when associated with G-65; L-68 and A-72. In Citrinine; leads to excitation and emission peaks of 516 and 529 nm, respectively; when associated with L-68; M-69 and A-72. In YFP 10C; shifts the major emission and exitation peak up to 20 nm; when associated with G-65; L-68 and A-72. In Topaz; shifts the major emission and exitation peak up to 20 nm; when associated with G-65; A-72 and R-79. In Venus; leads to yellow fluorescence, improved maturation and reduced environmental sensitivity; when associated with L-46; L-64; G-65; L-68; A-72; T-153; A-163 and G-175. 5 Publications1
Mutagenesisi206A → K: Abolishes the tendency to dimerize and leads to monomeric fluorescent proteins. 1 Publication1
Mutagenesisi206A → V in EBFP1.2; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; F-145; V-171 and S-198. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; F-145; I-150; V-155; V-171; S-198 and V-206. 1
Mutagenesisi222E → G: Suppresses the 399 nm excitation peak, leaving only the longer wavelength peak at 475 nm. 1 Publication1
Mutagenesisi224V → R in Azurite; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with H-66; R-80; F-145 and I-150. In EBFP2.0; shifts the excitation and emission spectra to shorter wavelengths and increases quantum yields compared to BFP; when associated with R-30; N-39; H-66; A-72; T-105; V-128; F-145; I-150; V-155; V-171; S-198 and V-206. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001925761 – 238Green fluorescent proteinAdd BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki65 ↔ 675-imidazolinone (Ser-Gly)1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei66(Z)-2,3-didehydrotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Contains a chromophore consisting of modified amino acid residues. The chromophore is formed by autocatalytic backbone condensation between Ser-65 and Gly-67, and oxidation of Tyr-66 to didehydrotyrosine. Maturation of the chromophore requires nothing other than molecular oxygen.1 Publication

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P42212

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Photocytes.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P42212, 1 interactor

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P42212

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P42212

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P42212

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the GFP family.Curated

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009017 GFP
IPR011584 GFP-related
IPR000786 Green_fluorescent_prot

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01353 GFP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01229 GFLUORESCENT

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54511 SSF54511, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P42212-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKFICTT
60 70 80 90 100
GKLPVPWPTL VTTFSYGVQC FSRYPDHMKQ HDFFKSAMPE GYVQERTIFF
110 120 130 140 150
KDDGNYKTRA EVKFEGDTLV NRIELKGIDF KEDGNILGHK LEYNYNSHNV
160 170 180 190 200
YIMADKQKNG IKVNFKIRHN IEDGSVQLAD HYQQNTPIGD GPVLLPDNHY
210 220 230
LSTQSALSKD PNEKRDHMVL LEFVTAAGIT HGMDELYK
Length:238
Mass (Da):26,886
Last modified:November 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEA5A6F21FBFB6E05
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2S → G in CAA65278 (PubMed:9154981).Curated1
Sequence conflicti25H → Q in CAA65278 (PubMed:9154981).Curated1
Sequence conflicti80Q → R in CAA65278 (PubMed:9154981).Curated1
Sequence conflicti157Q → P in AAA58246 (PubMed:8137953).Curated1
Sequence conflicti172E → K in AAA58246 (PubMed:8137953).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti100F → Y1 Publication1
Natural varianti108T → S1 Publication1
Natural varianti141L → M1 Publication1
Natural varianti219V → I1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M62654 mRNA Translation: AAA27722.1
M62653 mRNA Translation: AAA27721.1
L29345 mRNA Translation: AAA58246.1
X96418 mRNA Translation: CAA65278.1
U73901 Genomic DNA Translation: AAB18957.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JS0692 JQ1514

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

The greenest of us all - Issue 11 of June 2001

Protein Spotlight

Paint my thoughts - Issue 108 of August 2009

Wikipedia

Green fluorescent protein entry

Protein Spotlight

Paint my thoughts - Issue 108 of November 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62654 mRNA Translation: AAA27722.1
M62653 mRNA Translation: AAA27721.1
L29345 mRNA Translation: AAA58246.1
X96418 mRNA Translation: CAA65278.1
U73901 Genomic DNA Translation: AAB18957.1
PIRiJS0692 JQ1514

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9CX-ray2.40A/B/C/D1-238[»]
1BFPX-ray2.10A1-238[»]
1C4FX-ray2.25A1-238[»]
1CV7X-ray2.50A1-228[»]
1EMAX-ray1.90A1-238[»]
1EMBX-ray2.13A1-238[»]
1EMCX-ray2.30A/B/C/D2-237[»]
1EMEX-ray2.50A2-237[»]
1EMFX-ray2.40A2-238[»]
1EMGX-ray2.00A1-229[»]
1EMKX-ray2.10A2-237[»]
1EMLX-ray2.30A2-237[»]
1EMMX-ray2.30A2-238[»]
1F09X-ray2.14A1-238[»]
1F0BX-ray2.10A1-238[»]
1GFLX-ray1.90A/B2-238[»]
1H6RX-ray1.50A/B/C1-238[»]
1HCJX-ray1.80A/B/C/D1-238[»]
1HUYX-ray2.20A2-238[»]
1JBYX-ray1.80A1-238[»]
1JBZX-ray1.50A1-238[»]
1JC0X-ray2.00A/B/C1-238[»]
1JC1X-ray1.90A/B/C1-238[»]
1KP5X-ray2.60A/B1-238[»]
1KYPX-ray1.35A2-238[»]
1KYRX-ray1.50A2-238[»]
1KYSX-ray1.44A2-238[»]
1MYWX-ray2.20A2-238[»]
1Q4AX-ray1.45A1-238[»]
1Q4BX-ray1.48A1-238[»]
1Q4CX-ray1.55A1-238[»]
1Q4DX-ray1.58A1-238[»]
1Q4EX-ray1.38A1-238[»]
1Q73X-ray1.60A1-238[»]
1QXTX-ray2.00A2-229[»]
1QY3X-ray2.00A1-229[»]
1QYFX-ray1.50A1-227[»]
1QYOX-ray1.80A1-238[»]
1QYQX-ray1.80A2-238[»]
1RM9X-ray2.90A2-236[»]
1RMMX-ray1.90A2-227[»]
1RMOX-ray1.80A2-236[»]
1RMPX-ray3.00A2-229[»]
1RRXX-ray2.10A2-227[»]
1S6ZX-ray1.50A1-238[»]
1W7SX-ray1.85A/B/C/D1-238[»]
1W7TX-ray1.85A/B/C/D1-238[»]
1W7UX-ray1.85A/B/C/D1-238[»]
1YFPX-ray2.50A/B3-229[»]
1YHGX-ray2.50A/B2-238[»]
1YHHX-ray1.50A2-238[»]
1YHIX-ray1.90A2-238[»]
1YJ2X-ray1.50A2-238[»]
1YJFX-ray1.35A2-238[»]
1Z1PX-ray2.00A1-238[»]
1Z1QX-ray1.50A1-238[»]
2AH8X-ray2.24A/B1-238[»]
2AHAX-ray1.98A/B1-238[»]
2AWJX-ray1.60A2-229[»]
2AWKX-ray1.15A1-229[»]
2AWLX-ray1.85A1-229[»]
2AWMX-ray1.70A1-229[»]
2B3PX-ray1.40A1-238[»]
2B3QX-ray2.30A/B/C/D1-238[»]
2DUEX-ray1.24A1-238[»]
2DUFX-ray1.50A1-238[»]
2DUGX-ray1.40A1-238[»]
2DUHX-ray1.20A1-238[»]
2DUIX-ray1.36A1-238[»]
2EMDX-ray2.00A1-238[»]
2EMNX-ray2.30A1-238[»]
2EMOX-ray2.60A1-238[»]
2FWQX-ray1.40A2-238[»]
2FZUX-ray1.25A2-238[»]
2G16X-ray2.00A2-64[»]
B67-238[»]
2G2SX-ray1.20A2-63[»]
B66-238[»]
2G3DX-ray1.35A2-63[»]
B66-238[»]
2G5ZX-ray1.80A2-65[»]
B66-238[»]
2G6EX-ray1.30A2-238[»]
2H6VX-ray1.47A2-238[»]
2H9WX-ray1.82A2-237[»]
2HCGX-ray1.35A2-238[»]
2HFCX-ray1.20A2-238[»]
2HGDX-ray1.60A2-238[»]
2HGYX-ray2.05A2-238[»]
2HJOX-ray1.25A1-238[»]
2HQZX-ray1.20A1-238[»]
2HRSX-ray1.40A1-238[»]
2JADX-ray2.70A1-238[»]
2O24X-ray1.45A2-238[»]
2O29X-ray1.80A2-238[»]
2O2BX-ray1.94A2-238[»]
2OKWX-ray1.90A/B/C/D/E/F1-238[»]
2OKYX-ray2.40A/B1-238[»]
2Q57X-ray2.00A1-238[»]
2Q6PX-ray2.10A1-238[»]
2QRFX-ray1.50A1-230[»]
2QT2X-ray1.31A1-238[»]
2QU1X-ray1.70A1-238[»]
2QZ0X-ray1.20A2-229[»]
2WSNX-ray1.37A2-238[»]
2WSOX-ray1.15A2-238[»]
2WURX-ray0.90A1-237[»]
2Y0GX-ray1.50A2-238[»]
2YDZX-ray1.59A2-238[»]
2YE0X-ray1.47A2-238[»]
2YE1X-ray1.63A2-238[»]
2YFPX-ray2.60A1-238[»]
3AI4X-ray1.60A1-230[»]
3CB9X-ray1.31A2-238[»]
3CBEX-ray1.49A2-238[»]
3CD1X-ray1.31A2-238[»]
3CD9X-ray1.50A2-238[»]
3DPWX-ray1.59A2-238[»]
3DPXX-ray1.50A2-238[»]
3DPZX-ray1.70A2-238[»]
3DQ1X-ray1.70A2-238[»]
3DQ2X-ray1.60A2-238[»]
3DQ3X-ray1.70A2-238[»]
3DQ4X-ray1.47A2-238[»]
3DQ5X-ray1.50A2-238[»]
3DQ6X-ray1.60A2-238[»]
3DQ7X-ray1.23A2-238[»]
3DQ8X-ray1.51A2-238[»]
3DQ9X-ray1.40A2-238[»]
3DQAX-ray1.44A2-238[»]
3DQCX-ray1.49A2-238[»]
3DQDX-ray1.40A2-238[»]
3DQEX-ray1.43A2-238[»]
3DQFX-ray1.46A2-238[»]
3DQHX-ray1.45A2-238[»]
3DQIX-ray1.42A2-238[»]
3DQJX-ray1.51A2-238[»]
3DQKX-ray1.40A2-238[»]
3DQLX-ray1.47A2-238[»]
3DQMX-ray1.44A2-238[»]
3DQNX-ray1.44A2-238[»]
3DQOX-ray1.50A2-238[»]
3DQUX-ray1.42A2-238[»]
3ED8X-ray2.70A/B/C/D/E2-238[»]
3EK4X-ray2.65A2-238[»]
3EK7X-ray1.85A2-238[»]
3EK8X-ray2.80A2-238[»]
3EKHX-ray2.00A2-238[»]
3EKJX-ray2.80A2-238[»]
3EVPX-ray1.45A2-144[»]
3EVRX-ray2.00A2-144[»]
3EVUX-ray1.75A2-144[»]
3EVVX-ray2.60A2-238[»]
3G9AX-ray1.61A1-238[»]
3GEXX-ray1.60A1-238[»]
3GJ1X-ray1.80A/B/C/D1-230[»]
3GJ2X-ray1.90A/B/C/D1-230[»]
3I19X-ray1.36A1-238[»]
3K1KX-ray2.15A/B1-238[»]
3LA1X-ray1.29A1-238[»]
3O77X-ray2.35A2-238[»]
3O78X-ray2.60A/B2-237[»]
3OGOX-ray2.80A/B/C/D1-238[»]
3OSQX-ray1.90A2-238[»]
3OSRX-ray2.00A/B2-238[»]
3P28X-ray1.80A3-229[»]
3SG2X-ray2.00A2-238[»]
3SG3X-ray2.10A2-238[»]
3SG4X-ray2.40A2-238[»]
3SG5X-ray1.90A2-238[»]
3SG6X-ray1.70A2-238[»]
3SG7X-ray1.90A2-238[»]
3SRYX-ray1.16A2-238[»]
3SS0X-ray1.49A2-238[»]
3SSHX-ray1.28A2-238[»]
3SSKX-ray1.36A2-238[»]
3SSLX-ray1.45A2-238[»]
3SSPX-ray1.63A2-238[»]
3SSTX-ray1.40A2-238[»]
3SSVX-ray1.86A2-238[»]
3SSYX-ray1.77A2-238[»]
3ST0X-ray1.19A2-238[»]
3SV5X-ray1.53A2-238[»]
3SVBX-ray1.30A2-238[»]
3SVCX-ray1.31A2-238[»]
3SVDX-ray1.78A2-238[»]
3SVEX-ray1.49A2-238[»]
3U8PX-ray2.75A/B/C2-238[»]
3UFZX-ray1.85A2-229[»]
3UG0X-ray2.09A2-229[»]
3V3DX-ray1.95A2-238[»]
3VHTX-ray2.40A1-230[»]
3W1CX-ray1.30A2-238[»]
3W1DX-ray1.50A2-238[»]
3WLCX-ray2.49A2-238[»]
3WLDX-ray2.70A2-144[»]
3ZTFX-ray1.31A2-238[»]
4ANJX-ray2.60A1-238[»]
4AR7X-ray1.23A2-238[»]
4AS8X-ray1.02A2-238[»]
4B5YX-ray1.45A2-238[»]
4BDUX-ray3.00A/B/C/D1-230[»]
4EN1X-ray1.62A/B2-238[»]
4EULX-ray1.35A2-238[»]
4GESX-ray1.23B1-238[»]
4GF6X-ray1.10B1-237[»]
4H47X-ray1.90A1-238[»]
4H48X-ray1.45A1-238[»]
4IK1X-ray2.00A2-144[»]
4IK3X-ray2.01A149-238[»]
A2-142[»]
4IK4X-ray2.01A2-142[»]
A149-238[»]
4IK5X-ray2.50A2-142[»]
A149-238[»]
4IK8X-ray1.55A2-144[»]
A149-238[»]
4IK9X-ray1.80A2-144[»]
4J88X-ray2.08A/B2-238[»]
4J89X-ray2.10A/B2-238[»]
4J8AX-ray1.26A2-238[»]
4JFGX-ray3.00A/B/C/D/E/F/G/H1-238[»]
4JRBX-ray2.41A1-229[»]
4KA9X-ray1.58A5-238[»]
4KAGX-ray1.12A1-238[»]
4KEXX-ray1.60A1-238[»]
4KF5X-ray2.60A/B1-196[»]
4KW4X-ray1.75A2-238[»]
4KW8X-ray2.46A2-238[»]
4KW9X-ray1.80A2-238[»]
4L12X-ray1.78A2-230[»]
4L13X-ray1.66A2-230[»]
4L1IX-ray1.20A2-230[»]
4LQTX-ray1.10A2-238[»]
4LQUX-ray1.60A/B/C/D2-238[»]
4LW5X-ray2.55A/B/C/D/E2-238[»]
4N3DX-ray1.34A/B1-230[»]
4NDJX-ray1.85A2-238[»]
4NDKX-ray2.30A/B2-238[»]
4OGSX-ray2.21A/B1-238[»]
4ORNX-ray1.71A/B2-238[»]
4P1QX-ray1.50A3-231[»]
4P7HX-ray3.20A/B5-238[»]
4PA0X-ray2.25A/B5-234[»]
4PFEX-ray2.60A/B2-229[»]
4U2VX-ray2.30A/B/C/D1-230[»]
4XBIX-ray2.01A/B2-230[»]
4XGYX-ray1.49A2-238[»]
4XL5X-ray2.00A2-238[»]
4XOVX-ray1.20A2-238[»]
4XOWX-ray1.25A2-238[»]
4XVPX-ray3.40A/B/C2-238[»]
4Z4KX-ray2.80A/B1-230[»]
4Z4MX-ray2.15A/B1-230[»]
4ZF3X-ray1.90A/B51-236[»]
4ZF4X-ray1.82A/B4-237[»]
4ZF5X-ray1.70A/B4-237[»]
5AQBX-ray1.37B2-231[»]
5B61X-ray3.12A/B/C/D/E/F1-238[»]
5DPGX-ray1.85A2-238[»]
5DPHX-ray1.42A/B2-238[»]
5DPIX-ray2.54A/B/C/D/E/F2-238[»]
5DPJX-ray2.50A/B/C/D2-238[»]
5DQBX-ray1.25A2-238[»]
5DQMX-ray1.30A2-238[»]
5DRFX-ray1.14A2-238[»]
5DRGX-ray1.14A2-238[»]
5DTXX-ray1.45A1-63[»]
A65-238[»]
5DTYX-ray1.50A1-63[»]
A65-238[»]
5DTZX-ray1.50A/B/C/D2-238[»]
5DU0X-ray2.35A/B/C/D2-238[»]
5EHUX-ray1.45A/B2-238[»]
5F9GX-ray2.77A2-144[»]
5FGUX-ray1.90A1-229[»]
5HBDX-ray1.65A1-238[»]
5HGEX-ray1.86A1-238[»]
5HW9X-ray3.00A1-238[»]
5HZOX-ray2.49A/B1-235[»]
5J2OX-ray1.50A2-238[»]
5J3NX-ray2.45A/B2-238[»]
5JZKX-ray1.90A/B3-238[»]
5JZLX-ray1.80A/B3-238[»]
5KTGX-ray2.80A/B1-230[»]
5LELX-ray3.10C/F/I2-238[»]
5LEMX-ray2.98C2-238[»]
5MA3X-ray1.70B2-238[»]
5MA4X-ray1.40B2-238[»]
5MA5X-ray1.85B/D2-238[»]
5MA6X-ray2.30A2-238[»]
5MA8X-ray2.35B/D2-238[»]
5MA9X-ray1.57B/D/F/H2-238[»]
5MADX-ray1.53B/D/F/H2-238[»]
5MAKX-ray2.50B/D2-238[»]
5MSEX-ray1.66A/B/C/D2-238[»]
5N9OX-ray1.53A2-238[»]
5O89X-ray1.70A2-238[»]
5O8BX-ray1.70A2-238[»]
5O8CX-ray1.70A2-238[»]
5OX8X-ray1.29A2-238[»]
5OX9X-ray1.56A2-238[»]
5OXAX-ray1.16A2-238[»]
5OXBX-ray1.38A2-238[»]
5OXCX-ray1.02A1-238[»]
5T3IX-ray1.60A2-238[»]
5WJ2X-ray2.41A/B2-238[»]
5WJ3X-ray1.35A/B3-238[»]
5WJ4X-ray1.63A/B3-238[»]
6AS9X-ray1.75A1-238[»]
6B7RX-ray1.73A/B2-214[»]
6B7TX-ray1.91A/B3-194[»]
A/B214-237[»]
6FWWX-ray1.13A2-238[»]
6MB2electron microscopy5.00a/b/c/d/e/f/g/h/i/j/k/l/m/n/o2-229[»]
ProteinModelPortaliP42212
SMRiP42212
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP42212, 1 interactor

Proteomic databases

PRIDEiP42212

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-20291

Miscellaneous databases

EvolutionaryTraceiP42212

Family and domain databases

InterProiView protein in InterPro
IPR009017 GFP
IPR011584 GFP-related
IPR000786 Green_fluorescent_prot
PfamiView protein in Pfam
PF01353 GFP, 1 hit
PRINTSiPR01229 GFLUORESCENT
SUPFAMiSSF54511 SSF54511, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGFP_AEQVI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P42212
Secondary accession number(s): Q17104, Q27903, Q93125
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 7, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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