(cache) GFP - Green fluorescent protein - Aequorea victoria (Jellyfish)

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

bioluminescence
Source: UniProtKB
Traceable author statementⁱ
- 8137953
generation of precursor metabolites and energy
Source: UniProtKB
Traceable author statementⁱ
- 8137953
protein-chromophore linkage Source: UniProtKB-KW

Complete GO annotation...

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Green fluorescent protein
Gene namesⁱ	Name:GFP
Organismⁱ	Aequorea victoria (Jellyfish)
Taxonomic identifierⁱ	6100 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Cnidaria › Hydrozoa › Hydroidolina › Leptothecata › Aequoreidae › Aequorea

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 key	Position(s)	Length	Description
Mutagenesisⁱ	65 – 65	1	S → G in mut3; highly fluorescent mutant when excited at 488 nm; when associated with A-72. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	65 – 65	1	S → T: Increases fluoresence, photostability and shift the major exitation peak to 488 nm. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	72 – 72	1	S → A in mut3; highly fluorescent mutant when excited at 488 nm; when associated with G-65. 1 Publication Manual assertion based on experiment inⁱ Ref.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.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 238	238	Green fluorescent protein		PRO_0000192576	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Cross-linkⁱ	65 ↔ 67		5-imidazolinone (Ser-Gly)
Modified residueⁱ	66 – 66	1	(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

PRIDEⁱ	P42212.

PRIDEⁱ

P42212.

Expressionⁱ

Tissue specificityⁱ

Photocytes.

Interactionⁱ

Subunit structureⁱ

Monomer.

Protein-protein interaction databases

IntActⁱ	P42212. 1 interaction.

IntActⁱ

P42212. 1 interaction.

Structureⁱ

Secondary structure

1

238

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Helixⁱ	4 – 8	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	12 – 22	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	25 – 36	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Helixⁱ	37 – 39	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	41 – 48	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Helixⁱ	57 – 60	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Turnⁱ	61 – 63	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Turnⁱ	65 – 67	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1QYO
Helixⁱ	69 – 71	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Helixⁱ	76 – 81	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Helixⁱ	83 – 86	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Turnⁱ	87 – 90	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	92 – 100	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	105 – 115	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	118 – 128	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	132 – 134	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1EMK
Turnⁱ	135 – 139	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	149 – 155	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Helixⁱ	156 – 158	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	160 – 171	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Turnⁱ	172 – 174	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:4OGS
Beta strandⁱ	176 – 191	16	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	198 – 208	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Beta strandⁱ	217 – 227	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2WUR
Helixⁱ	233 – 236	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:4GF6

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

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	[»]
4IK5	X-ray	2.50	A	2-142	[»]
			A	149-238	[»]
4IK8	X-ray	1.55	A	2-144	[»]
			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	[»]
4NDJ	X-ray	1.85	A	2-238	[»]
4NDK	X-ray	2.30	A/B	2-238	[»]
4OGS	X-ray	2.21	A/B	1-238	[»]
4ORN	X-ray	1.71	A/B	2-238	[»]
4P1Q	X-ray	1.50	A	3-231	[»]
4P7H	X-ray	3.20	A/B	5-238	[»]
4PFE	X-ray	2.60	A/B	2-229	[»]
4U2V	X-ray	2.30	A/B/C/D	1-230	[»]
4XGY	X-ray	1.49	A	2-238	[»]
4ZF3	X-ray	1.90	A/B	51-236	[»]
4ZF4	X-ray	1.82	A/B	51-237	[»]
4ZF5	X-ray	1.70	A/B	51-237	[»]

ProteinModelPortalⁱ

P42212.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P42212.

EvolutionaryTraceⁱ

P42212.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the GFP family.Curated

Family and domain databases

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

Sequenceⁱ

Sequence statusⁱ: Complete.

P42212-1 [UniParc]FASTA Add to basket

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        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 key	Position(s)	Length	Description
Sequence conflictⁱ	2 – 2	1	S → G in CAA65278 (PubMed:9154981).Curated
Sequence conflictⁱ	25 – 25	1	H → Q in CAA65278 (PubMed:9154981).Curated
Sequence conflictⁱ	80 – 80	1	Q → R in CAA65278 (PubMed:9154981).Curated
Sequence conflictⁱ	157 – 157	1	Q → P in AAA58246 (PubMed:8137953).Curated
Sequence conflictⁱ	172 – 172	1	E → K in AAA58246 (PubMed:8137953).Curated

Natural variant

Feature key	Position(s)	Length	Description
Natural variantⁱ	100 – 100	1	F → Y.1 Publication Manual assertion based on experiment inⁱ Ref.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.
Natural variantⁱ	108 – 108	1	T → S.1 Publication Manual assertion based on experiment inⁱ Ref.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.
Natural variantⁱ	141 – 141	1	L → M.1 Publication Manual assertion based on experiment inⁱ Ref.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.
Natural variantⁱ	219 – 219	1	V → I.1 Publication Manual assertion based on experiment inⁱ Ref.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.

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.
PIRⁱ	JS0692. 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.
PIRⁱ	JS0692. JQ1514.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

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	[»]
4IK5	X-ray	2.50	A	2-142	[»]
			A	149-238	[»]
4IK8	X-ray	1.55	A	2-144	[»]
			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	[»]
4NDJ	X-ray	1.85	A	2-238	[»]
4NDK	X-ray	2.30	A/B	2-238	[»]
4OGS	X-ray	2.21	A/B	1-238	[»]
4ORN	X-ray	1.71	A/B	2-238	[»]
4P1Q	X-ray	1.50	A	3-231	[»]
4P7H	X-ray	3.20	A/B	5-238	[»]
4PFE	X-ray	2.60	A/B	2-229	[»]
4U2V	X-ray	2.30	A/B/C/D	1-230	[»]
4XGY	X-ray	1.49	A	2-238	[»]
4ZF3	X-ray	1.90	A/B	51-236	[»]
4ZF4	X-ray	1.82	A/B	51-237	[»]
4ZF5	X-ray	1.70	A/B	51-237	[»]

ProteinModelPortalⁱ

P42212.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

IntActⁱ	P42212. 1 interaction.

IntActⁱ

P42212. 1 interaction.

Proteomic databases

PRIDEⁱ	P42212.

PRIDEⁱ

P42212.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P42212.

EvolutionaryTraceⁱ

P42212.

Family and domain databases

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

Publicationsⁱ

"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.
"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].
"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].
"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.
"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.
"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.
"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.
"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).
"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.
"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).

+Additional computationally mapped references.

Entry informationⁱ

Entry nameⁱ

GFP_AEQVI

Accessionⁱ

Primary (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:	September 16, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing

Documents

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

External Data

Dasty 3

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 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.

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UniProtKB - P42212 (GFP_AEQVI)

UniProt

P42212 - GFP_AEQVI

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Green fluorescent protein

GFP

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

<p>Describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.</p><p><a href='../manual/biophysicochemical_properties' target='_top'>More...</a></p>Absorptioni

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

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

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>Describes the use of a specific protein in the biotechnological industry.</p><p><a href='../manual/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

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

Molecule processing

Amino acid modifications

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

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

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

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

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Natural variant

Sequence databases

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

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Sequence databases

3D structure databases

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Miscellaneous databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsi

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

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

Documents

External Data

Functionⁱ

Absorptionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

Biotechnological useⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Web resourcesⁱ

Publicationsⁱ

Entry informationⁱ

Miscellaneousⁱ