Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P42212

- GFP_AEQVI

UniProt

P42212 - GFP_AEQVI

Protein

Green fluorescent protein

Gene

GFP

Organism
Aequorea victoria (Jellyfish)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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[»]
    4IK3X-ray2.01A149-238[»]
    A2-142[»]
    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[»]
    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[»]
    4OGSX-ray2.21A/B1-238[»]
    4P7HX-ray3.20A/B5-238[»]
    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

    MSKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKFICTT    50
    GKLPVPWPTL VTTFSYGVQC FSRYPDHMKQ HDFFKSAMPE GYVQERTIFF 100
    KDDGNYKTRA EVKFEGDTLV NRIELKGIDF KEDGNILGHK LEYNYNSHNV 150
    YIMADKQKNG IKVNFKIRHN IEDGSVQLAD HYQQNTPIGD GPVLLPDNHY 200
    LSTQSALSKD PNEKRDHMVL LEFVTAAGIT HGMDELYK 238
    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 [» ]
    4IK3 X-ray 2.01 A 149-238 [» ]
    A 2-142 [» ]
    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 [» ]
    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 [» ]
    4OGS X-ray 2.21 A/B 1-238 [» ]
    4P7H X-ray 3.20 A/B 5-238 [» ]
    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 1, 2014
    This is version 121 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