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P42212

- GFP_AEQVI

UniProt

P42212 - GFP_AEQVI

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Protein

Green fluorescent protein

Gene

GFP

Organism
Aequorea victoria (Jellyfish)
Status
Reviewed - 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 nm

Exhibits a smaller absorbance peak at 470 nm. The fluorescence emission spectrum peaks at 509 nm with a shoulder at 540 nm.

GO - Biological processi

  1. bioluminescence Source: UniProtKB
  2. generation of precursor metabolites and energy Source: UniProtKB
  3. protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Photoprotein

Keywords - Biological processi

Luminescence

Keywords - Ligandi

Chromophore

Names & Taxonomyi

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

Pathology & Biotechi

Biotechnological usei

Green fluorescent protein has been engineered to produce a vast number of variously colored mutants, fusion proteins, and biosensors. Fluorescent proteins and its mutated allelic forms, blue, cyan and yellow 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.1 Publication
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651S → G in mut3; highly fluorescent mutant when excited at 488 nm; when associated with A-72. 1 Publication
Mutagenesisi65 – 651S → T: Increases fluoresence, photostability and shift the major exitation peak to 488 nm. 1 Publication
Mutagenesisi72 – 721S → A in mut3; highly fluorescent mutant when excited at 488 nm; when associated with G-65. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Green fluorescent proteinPRO_0000192576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki65 ↔ 675-imidazolinone (Ser-Gly)
Modified residuei66 – 661(Z)-2,3-didehydrotyrosine

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.

Proteomic databases

PRIDEiP42212.

Expressioni

Tissue specificityi

Photocytes.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP42212. 1 interaction.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85
Beta strandi12 – 2211
Beta strandi25 – 3612
Helixi37 – 393
Beta strandi41 – 488
Helixi57 – 604
Turni61 – 633
Turni65 – 673
Helixi69 – 713
Helixi76 – 816
Helixi83 – 864
Turni87 – 904
Beta strandi92 – 1009
Beta strandi105 – 11511
Beta strandi118 – 12811
Beta strandi132 – 1343
Turni135 – 1395
Beta strandi141 – 1433
Beta strandi149 – 1557
Helixi156 – 1583
Beta strandi160 – 17112
Turni172 – 1743
Beta strandi176 – 19116
Beta strandi198 – 20811
Beta strandi217 – 22711
Helixi233 – 2364

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
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[»]
4OGSX-ray2.21A/B1-238[»]
4P1QX-ray1.50A3-231[»]
4P7HX-ray3.20A/B5-238[»]
4U2VX-ray2.30A/B/C/D1-230[»]
ProteinModelPortaliP42212.
SMRiP42212. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42212.

Family & Domainsi

Sequence similaritiesi

Belongs to the GFP family.Curated

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR009017. GFP.
IPR011584. GFP-related.
IPR023413. GFP_like.
IPR000786. Green_fluorescent_prot.
[Graphical view]
PfamiPF01353. GFP. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → G in CAA65278. (PubMed:9154981)Curated
Sequence conflicti25 – 251H → Q in CAA65278. (PubMed:9154981)Curated
Sequence conflicti80 – 801Q → R in CAA65278. (PubMed:9154981)Curated
Sequence conflicti157 – 1571Q → P in AAA58246. (PubMed:8137953)Curated
Sequence conflicti172 – 1721E → K in AAA58246. (PubMed:8137953)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001F → Y.1 Publication
Natural varianti108 – 1081T → S.1 Publication
Natural varianti141 – 1411L → M.1 Publication
Natural varianti219 – 2191V → I.1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi JS0692. JQ1514.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B9C X-ray 2.40 A/B/C/D 1-238 [» ]
1BFP X-ray 2.10 A 1-238 [» ]
1C4F X-ray 2.25 A 1-238 [» ]
1CV7 X-ray 2.50 A 1-228 [» ]
1EMA X-ray 1.90 A 1-238 [» ]
1EMB X-ray 2.13 A 1-238 [» ]
1EMC X-ray 2.30 A/B/C/D 2-237 [» ]
1EME X-ray 2.50 A 2-237 [» ]
1EMF X-ray 2.40 A 2-238 [» ]
1EMG X-ray 2.00 A 1-229 [» ]
1EMK X-ray 2.10 A 2-237 [» ]
1EML X-ray 2.30 A 2-237 [» ]
1EMM X-ray 2.30 A 2-238 [» ]
1F09 X-ray 2.14 A 1-238 [» ]
1F0B X-ray 2.10 A 1-238 [» ]
1GFL X-ray 1.90 A/B 2-238 [» ]
1H6R X-ray 1.50 A/B/C 1-238 [» ]
1HCJ X-ray 1.80 A/B/C/D 1-238 [» ]
1HUY X-ray 2.20 A 2-238 [» ]
1JBY X-ray 1.80 A 1-238 [» ]
1JBZ X-ray 1.50 A 1-238 [» ]
1JC0 X-ray 2.00 A/B/C 1-238 [» ]
1JC1 X-ray 1.90 A/B/C 1-238 [» ]
1KP5 X-ray 2.60 A/B 1-238 [» ]
1KYP X-ray 1.35 A 2-238 [» ]
1KYR X-ray 1.50 A 2-238 [» ]
1KYS X-ray 1.44 A 2-238 [» ]
1MYW X-ray 2.20 A 2-238 [» ]
1Q4A X-ray 1.45 A 1-238 [» ]
1Q4B X-ray 1.48 A 1-238 [» ]
1Q4C X-ray 1.55 A 1-238 [» ]
1Q4D X-ray 1.58 A 1-238 [» ]
1Q4E X-ray 1.38 A 1-238 [» ]
1Q73 X-ray 1.60 A 1-238 [» ]
1QXT X-ray 2.00 A 2-229 [» ]
1QY3 X-ray 2.00 A 1-229 [» ]
1QYF X-ray 1.50 A 1-227 [» ]
1QYO X-ray 1.80 A 1-238 [» ]
1QYQ X-ray 1.80 A 2-238 [» ]
1RM9 X-ray 2.90 A 2-236 [» ]
1RMM X-ray 1.90 A 2-227 [» ]
1RMO X-ray 1.80 A 2-236 [» ]
1RMP X-ray 3.00 A 2-229 [» ]
1RRX X-ray 2.10 A 2-227 [» ]
1S6Z X-ray 1.50 A 1-238 [» ]
1W7S X-ray 1.85 A/B/C/D 1-238 [» ]
1W7T X-ray 1.85 A/B/C/D 1-238 [» ]
1W7U X-ray 1.85 A/B/C/D 1-238 [» ]
1YFP X-ray 2.50 A/B 3-229 [» ]
1YHG X-ray 2.50 A/B 2-238 [» ]
1YHH X-ray 1.50 A 2-238 [» ]
1YHI X-ray 1.90 A 2-238 [» ]
1YJ2 X-ray 1.50 A 2-238 [» ]
1YJF X-ray 1.35 A 2-238 [» ]
1Z1P X-ray 2.00 A 1-238 [» ]
1Z1Q X-ray 1.50 A 1-238 [» ]
2AH8 X-ray 2.24 A/B 1-238 [» ]
2AHA X-ray 1.98 A/B 1-238 [» ]
2AWJ X-ray 1.60 A 2-229 [» ]
2AWK X-ray 1.15 A 1-229 [» ]
2AWL X-ray 1.85 A 1-229 [» ]
2AWM X-ray 1.70 A 1-229 [» ]
2B3P X-ray 1.40 A 1-238 [» ]
2B3Q X-ray 2.30 A/B/C/D 1-238 [» ]
2DUE X-ray 1.24 A 1-238 [» ]
2DUF X-ray 1.50 A 1-238 [» ]
2DUG X-ray 1.40 A 1-238 [» ]
2DUH X-ray 1.20 A 1-238 [» ]
2DUI X-ray 1.36 A 1-238 [» ]
2EMD X-ray 2.00 A 1-238 [» ]
2EMN X-ray 2.30 A 1-238 [» ]
2EMO X-ray 2.60 A 1-238 [» ]
2FWQ X-ray 1.40 A 2-238 [» ]
2FZU X-ray 1.25 A 2-238 [» ]
2G16 X-ray 2.00 A 2-64 [» ]
B 67-238 [» ]
2G2S X-ray 1.20 A 2-63 [» ]
B 66-238 [» ]
2G3D X-ray 1.35 A 2-63 [» ]
B 66-238 [» ]
2G5Z X-ray 1.80 A 2-65 [» ]
B 66-238 [» ]
2G6E X-ray 1.30 A 2-238 [» ]
2H6V X-ray 1.47 A 2-238 [» ]
2H9W X-ray 1.82 A 2-237 [» ]
2HCG X-ray 1.35 A 2-238 [» ]
2HFC X-ray 1.20 A 2-238 [» ]
2HGD X-ray 1.60 A 2-238 [» ]
2HGY X-ray 2.05 A 2-238 [» ]
2HJO X-ray 1.25 A 1-238 [» ]
2HQZ X-ray 1.20 A 1-238 [» ]
2HRS X-ray 1.40 A 1-238 [» ]
2JAD X-ray 2.70 A 1-238 [» ]
2O24 X-ray 1.45 A 2-238 [» ]
2O29 X-ray 1.80 A 2-238 [» ]
2O2B X-ray 1.94 A 2-238 [» ]
2OKW X-ray 1.90 A/B/C/D/E/F 1-238 [» ]
2OKY X-ray 2.40 A/B 1-238 [» ]
2Q57 X-ray 2.00 A 1-238 [» ]
2Q6P X-ray 2.10 A 1-238 [» ]
2QRF X-ray 1.50 A 1-230 [» ]
2QT2 X-ray 1.31 A 1-238 [» ]
2QU1 X-ray 1.70 A 1-238 [» ]
2QZ0 X-ray 1.20 A 2-229 [» ]
2WSN X-ray 1.37 A 2-238 [» ]
2WSO X-ray 1.15 A 2-238 [» ]
2WUR X-ray 0.90 A 1-237 [» ]
2Y0G X-ray 1.50 A 2-238 [» ]
2YDZ X-ray 1.59 A 2-238 [» ]
2YE0 X-ray 1.47 A 2-238 [» ]
2YE1 X-ray 1.63 A 2-238 [» ]
2YFP X-ray 2.60 A 1-238 [» ]
3CB9 X-ray 1.31 A 2-238 [» ]
3CBE X-ray 1.49 A 2-238 [» ]
3CD1 X-ray 1.31 A 2-238 [» ]
3CD9 X-ray 1.50 A 2-238 [» ]
3DPW X-ray 1.59 A 2-238 [» ]
3DPX X-ray 1.50 A 2-238 [» ]
3DPZ X-ray 1.70 A 2-238 [» ]
3DQ1 X-ray 1.70 A 2-238 [» ]
3DQ2 X-ray 1.60 A 2-238 [» ]
3DQ3 X-ray 1.70 A 2-238 [» ]
3DQ4 X-ray 1.47 A 2-238 [» ]
3DQ5 X-ray 1.50 A 2-238 [» ]
3DQ6 X-ray 1.60 A 2-238 [» ]
3DQ7 X-ray 1.23 A 2-238 [» ]
3DQ8 X-ray 1.51 A 2-238 [» ]
3DQ9 X-ray 1.40 A 2-238 [» ]
3DQA X-ray 1.44 A 2-238 [» ]
3DQC X-ray 1.49 A 2-238 [» ]
3DQD X-ray 1.40 A 2-238 [» ]
3DQE X-ray 1.43 A 2-238 [» ]
3DQF X-ray 1.46 A 2-238 [» ]
3DQH X-ray 1.45 A 2-238 [» ]
3DQI X-ray 1.42 A 2-238 [» ]
3DQJ X-ray 1.51 A 2-238 [» ]
3DQK X-ray 1.40 A 2-238 [» ]
3DQL X-ray 1.47 A 2-238 [» ]
3DQM X-ray 1.44 A 2-238 [» ]
3DQN X-ray 1.44 A 2-238 [» ]
3DQO X-ray 1.50 A 2-238 [» ]
3DQU X-ray 1.42 A 2-238 [» ]
3ED8 X-ray 2.70 A/B/C/D/E 2-238 [» ]
3EK4 X-ray 2.65 A 2-238 [» ]
3EK7 X-ray 1.85 A 2-238 [» ]
3EK8 X-ray 2.80 A 2-238 [» ]
3EKH X-ray 2.00 A 2-238 [» ]
3EKJ X-ray 2.80 A 2-238 [» ]
3EVP X-ray 1.45 A 2-144 [» ]
3EVR X-ray 2.00 A 2-144 [» ]
3EVU X-ray 1.75 A 2-144 [» ]
3EVV X-ray 2.60 A 2-238 [» ]
3G9A X-ray 1.61 A 1-238 [» ]
3GEX X-ray 1.60 A 1-238 [» ]
3GJ1 X-ray 1.80 A/B/C/D 1-230 [» ]
3GJ2 X-ray 1.90 A/B/C/D 1-230 [» ]
3I19 X-ray 1.36 A 1-238 [» ]
3K1K X-ray 2.15 A/B 1-238 [» ]
3LA1 X-ray 1.29 A 1-238 [» ]
3O77 X-ray 2.35 A 2-238 [» ]
3O78 X-ray 2.60 A/B 2-237 [» ]
3OGO X-ray 2.80 A/B/C/D 1-238 [» ]
3OSQ X-ray 1.90 A 2-238 [» ]
3OSR X-ray 2.00 A/B 2-238 [» ]
3P28 X-ray 1.80 A 3-229 [» ]
3SG2 X-ray 2.00 A 2-238 [» ]
3SG3 X-ray 2.10 A 2-238 [» ]
3SG4 X-ray 2.40 A 2-238 [» ]
3SG5 X-ray 1.90 A 2-238 [» ]
3SG6 X-ray 1.70 A 2-238 [» ]
3SG7 X-ray 1.90 A 2-238 [» ]
3SRY X-ray 1.16 A 2-238 [» ]
3SS0 X-ray 1.49 A 2-238 [» ]
3SSH X-ray 1.28 A 2-238 [» ]
3SSK X-ray 1.36 A 2-238 [» ]
3SSL X-ray 1.45 A 2-238 [» ]
3SSP X-ray 1.63 A 2-238 [» ]
3SST X-ray 1.40 A 2-238 [» ]
3SSV X-ray 1.86 A 2-238 [» ]
3SSY X-ray 1.77 A 2-238 [» ]
3ST0 X-ray 1.19 A 2-238 [» ]
3SV5 X-ray 1.53 A 2-238 [» ]
3SVB X-ray 1.30 A 2-238 [» ]
3SVC X-ray 1.31 A 2-238 [» ]
3SVD X-ray 1.78 A 2-238 [» ]
3SVE X-ray 1.49 A 2-238 [» ]
3U8P X-ray 2.75 A/B/C 2-238 [» ]
3UFZ X-ray 1.85 A 2-229 [» ]
3UG0 X-ray 2.09 A 2-229 [» ]
3V3D X-ray 1.95 A 2-238 [» ]
3VHT X-ray 2.40 A 1-230 [» ]
3W1C X-ray 1.30 A 2-238 [» ]
3W1D X-ray 1.50 A 2-238 [» ]
3WLC X-ray 2.49 A 2-238 [» ]
3WLD X-ray 2.70 A 2-144 [» ]
3ZTF X-ray 1.31 A 2-238 [» ]
4ANJ X-ray 2.60 A 1-238 [» ]
4AR7 X-ray 1.23 A 2-238 [» ]
4AS8 X-ray 1.02 A 2-238 [» ]
4B5Y X-ray 1.45 A 2-238 [» ]
4BDU X-ray 3.00 A/B/C/D 1-230 [» ]
4EN1 X-ray 1.62 A/B 2-238 [» ]
4EUL X-ray 1.35 A 2-238 [» ]
4GES X-ray 1.23 B 1-238 [» ]
4GF6 X-ray 1.10 B 1-237 [» ]
4H47 X-ray 1.90 A 1-238 [» ]
4H48 X-ray 1.45 A 1-238 [» ]
4IK1 X-ray 2.00 A 2-144 [» ]
4IK3 X-ray 2.01 A 149-238 [» ]
A 2-142 [» ]
4IK4 X-ray 2.01 A 2-142 [» ]
A 149-238 [» ]
4IK9 X-ray 1.80 A 2-144 [» ]
4J88 X-ray 2.08 A/B 2-238 [» ]
4J89 X-ray 2.10 A/B 2-238 [» ]
4J8A X-ray 1.26 A 2-238 [» ]
4JFG X-ray 3.00 A/B/C/D/E/F/G/H 1-238 [» ]
4JRB X-ray 2.41 A 1-229 [» ]
4KA9 X-ray 1.58 A 5-238 [» ]
4KAG X-ray 1.12 A 1-238 [» ]
4KEX X-ray 1.60 A 1-238 [» ]
4KF5 X-ray 2.60 A/B 1-196 [» ]
4KW4 X-ray 1.75 A 2-238 [» ]
4KW8 X-ray 2.46 A 2-238 [» ]
4KW9 X-ray 1.80 A 2-238 [» ]
4L12 X-ray 1.78 A 2-230 [» ]
4L13 X-ray 1.66 A 2-230 [» ]
4L1I X-ray 1.20 A 2-230 [» ]
4LQT X-ray 1.10 A 2-238 [» ]
4LQU X-ray 1.60 A/B/C/D 2-238 [» ]
4LW5 X-ray 2.55 A/B/C/D/E 2-238 [» ]
4N3D X-ray 1.34 A/B 1-230 [» ]
4OGS X-ray 2.21 A/B 1-238 [» ]
4P1Q X-ray 1.50 A 3-231 [» ]
4P7H X-ray 3.20 A/B 5-238 [» ]
4U2V X-ray 2.30 A/B/C/D 1-230 [» ]
ProteinModelPortali P42212.
SMRi P42212. Positions 2-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P42212. 1 interaction.

Proteomic databases

PRIDEi P42212.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P42212.

Family and domain databases

Gene3Di 2.40.155.10. 1 hit.
InterProi IPR009017. GFP.
IPR011584. GFP-related.
IPR023413. GFP_like.
IPR000786. Green_fluorescent_prot.
[Graphical view ]
Pfami PF01353. GFP. 1 hit.
[Graphical view ]
PRINTSi PR01229. GFLUORESCENT.
SUPFAMi SSF54511. SSF54511. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Primary structure of the Aequorea victoria green-fluorescent protein."
    Prasher D.C., Eckenrode V.K., Ward W.W., Prendergast F.G., Cormier M.J.
    Gene 111:229-233(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS TYR-100; SER-108; MET-141 AND ILE-219.
  2. "Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein."
    Inouye S., Tsuji F.I.
    FEBS Lett. 341:277-280(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Enhanced expression in tobacco of the gene encoding green fluorescent protein by modification of its codon usage."
    Rouwendal G.J.A., Mendes O., Wolbert E.J.H., de Boer A.D.
    Plant Mol. Biol. 33:989-999(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "FACS-optimized mutants of the green fluorescent protein (GFP)."
    Cormack B.P., Valdivia R.H., Falkow S.
    Gene 173:33-38(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-65 AND SER-72.
  5. "Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein."
    Cody C.W., Prasher D.C., Westler W.M., Prendergast F.G., Ward W.W.
    Biochemistry 32:1212-1218(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOPHORE.
  6. "A molecular thermometer based on fluorescent protein blinking."
    Wong F.H., Banks D.S., Abu-Arish A., Fradin C.
    J. Am. Chem. Soc. 129:10302-10303(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY.
  7. "Crystal structure of the Aequorea victoria green fluorescent protein."
    Ormoe M., Cubitt A.B., Kallio K., Gross L.A., Tsien R.Y., Remington S.J.
    Science 273:1392-1395(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65.
  8. "The molecular structure of green fluorescent protein."
    Yang F., Moss L.G., Phillips G.N. Jr.
    Nat. Biotechnol. 14:1246-1251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  9. "Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein."
    Wachter R.M., Elsliger M.-A., Kallio K., Hanson G.T., Remington S.J.
    Structure 6:1267-1277(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT WITH YELLOW EMISSION.
  10. "Structural and spectral response of green fluorescent protein variants to changes in pH."
    Elsliger M.-A., Wachter R.M., Hanson G.T., Kallio K., Remington S.J.
    Biochemistry 38:5296-5301(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiGFP_AEQVI
AccessioniPrimary (citable) accession number: P42212
Secondary accession number(s): Q17104, Q27903, Q93125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 122 of the entry and version 1 of the sequence. [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

External Data

Dasty 3