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Protein

Green fluorescent protein

Gene

GFP

Organism
Aequorea victoria (Jellyfish)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

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

GO - Biological processi

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

Keywordsi

Molecular functionPhotoprotein
Biological processLuminescence
LigandChromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Green fluorescent protein
Gene namesi
Name:GFP
OrganismiAequorea victoria (Jellyfish)
Taxonomic identifieri6100 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaHydrozoaHydroidolinaLeptothecataAequoreidaeAequorea

Pathology & Biotechi

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
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001925761 – 238Green fluorescent proteinAdd BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki65 ↔ 675-imidazolinone (Ser-Gly)
Modified residuei66(Z)-2,3-didehydrotyrosine1

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

PRIDEiP42212.

Expressioni

Tissue specificityi

Photocytes.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP42212. 1 interactor.

Structurei

Secondary structure

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 8Combined sources5
Beta strandi12 – 22Combined sources11
Beta strandi25 – 36Combined sources12
Helixi37 – 39Combined sources3
Beta strandi41 – 48Combined sources8
Helixi57 – 60Combined sources4
Turni61 – 63Combined sources3
Turni65 – 67Combined sources3
Helixi69 – 71Combined sources3
Helixi76 – 81Combined sources6
Helixi83 – 86Combined sources4
Turni87 – 90Combined sources4
Beta strandi92 – 100Combined sources9
Beta strandi105 – 115Combined sources11
Beta strandi118 – 128Combined sources11
Beta strandi132 – 134Combined sources3
Turni135 – 139Combined sources5
Beta strandi141 – 147Combined sources7
Beta strandi149 – 155Combined sources7
Helixi156 – 158Combined sources3
Beta strandi160 – 171Combined sources12
Turni172 – 174Combined sources3
Beta strandi176 – 191Combined sources16
Beta strandi198 – 208Combined sources11
Beta strandi217 – 227Combined sources11
Helixi233 – 236Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
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[»]
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[»]
5KTGX-ray2.80A/B1-230[»]
5T3IX-ray1.60A2-238[»]
ProteinModelPortaliP42212.
SMRiP42212.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42212.

Family & Domainsi

Sequence similaritiesi

Belongs to the GFP family.Curated

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.

Sequencei

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
Checksum:iEA5A6F21FBFB6E05
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Natural varianti100F → Y1 Publication1
Natural varianti108T → S1 Publication1
Natural varianti141L → M1 Publication1
Natural varianti219V → I1 Publication1

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.

Cross-referencesi

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:
PDBei
RCSB PDBi
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[»]
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[»]
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[»]
5KTGX-ray2.80A/B1-230[»]
5T3IX-ray1.60A2-238[»]
ProteinModelPortaliP42212.
SMRiP42212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP42212. 1 interactor.

Proteomic databases

PRIDEiP42212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

Entry informationi

Entry nameiGFP_AEQVI
AccessioniPrimary (citable) accession number: P42212
Secondary accession number(s): Q17104, Q27903, Q93125
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 10, 2017
This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.