Post translational modifications

Da
Da
Type ID Name Description Educt Product pKa1 pKa2 pKa3 NativeCharge Loss Gain Deltamass UVSpec H AA Pattern
Custom 1 Custom
Create your own modification.
None None None Av: 0 M: 0
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
Glycosylation 2 N-Glycosylation
None None None H2O Av: 18.0153 M: 18.0106
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
N N(?=[^P][ST])
Predefined 3 Pyroglutamic Acid
Pyroglutamate formation occurs through the rearrangement of the originally synthesized glutamine residues at the N-terminus. Lit.
Pyroglutamic Acid reactants Pyroglutamic Acid products None None None NH3 Av: -17.0305 M: -17.0265
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
4 Q, ^ ^(?=Q)
Predefined 4 Disulfide bond
By default Prot pi handels proteins assuming all cystein side chains are reduced to free sulfhydryl. Disulfide bonds are usually formed in proteins secreted to the extracellular medium. Therefore disulfide bonds can be specified as a modification, so that cystein is treated as halfcystine. Lit.
Disulfide bond reactants Disulfide bond products None None None H Av: -1.0079 M: -1.0078
λ
/ nm
ε
/ M-1 cm-1
214 670
240 187
245 193.5
250 193
255 180.5
260 157.5
265 136
270 107
272 97.5
274 87.5
276 80
278 70
280 62.5
282 55
284 47.5
286 42.5
288 36.5
290 31.5
292 27
294 25
296 21.5
298 18
300 15.5
302 14.5
304 12
306 10
308 7.5
310 5
312 2.5
314 0
316 0
318 0
320 0
C
Predefined 5 Alkylation (iodoacetamide)
Iodoacetamide reacts covalently with the side-chain thiol group of cysteine. It is often used to modify SH-groups to prevent the re-formation of disulfide bonds after the reduction of cystine residues to cysteine.
Alkylation (iodoacetamide) reactants Alkylation (iodoacetamide) products None None None H C2H4NO Av: 57.0514 M: 57.0215
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
-3.8 C
Predefined 6 Alkylation (iodoacetic acid)
Iodoacetic acid reacts covalently with the side-chain thiol group of cysteine. It is often used to modify SH-groups to prevent the re-formation of disulfide bonds after the reduction of cystine residues to cysteine.
Alkylation (iodoacetic acid) reactants Alkylation (iodoacetic acid) products Acidic 3.2 None None H C2H3O2 Av: 58.0362 M: 58.0055
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
-1.7 C
Predefined 7 Deamidation (asparagine)
Nonenzymatic deamidation of asparagines is a common modification of proteins. Deamidation proceeding through the formation fo succinimide intermediate followed by hydrolysis results in the formation of isoaspartate and aspartate in a molar ratio of approximately 3:1.
Deamidation (asparagine) reactants Deamidation (asparagine) products Acidic 4.07 None None NH3 H2O Av: 0.9848 M: 0.984
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
4.08 N
Predefined 8 Glycation (glucose)
Glycation is the result of typically covalent bonding of a protein with a sugar molecule, such as fructose or glucose, without the controlling action of an enzyme. Glucose reacts with proteins through the formation of a Schiff base between the aldehyde group of glucose and the primary amines of lysine and the N-terminus of the protein.
Glycation (glucose) reactants Glycation (glucose) products None None None H2O C6H12O6 Av: 162.1408 M: 162.0528
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
K, ^
Predefined 9 Hydroxylation (proline)
Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). Hydroxyproline is a major component of the protein collagen and plays a key roles for collagen stability. The sequence of collagen often follows the pattern Gly-Xaa-Hyp.
Hydroxylation (proline) reactants Hydroxylation (proline) products None None None O Av: 15.9994 M: 15.9949
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
P (?<=G.)P
Predefined 10 Succinimide (asparagine)
Nonenzymatic deamidation of asparagines is a common modification of proteins. Deamidation proceeding through the formation fo succinimide intermediate followed by hydrolysis results in the formation of isoaspartate and aspartate in a molar ratio of apporximately 3:1.
Succinimide (asparagine) reactants Succinimide (asparagine) products None None None NH3 Av: -17.0305 M: -17.0265
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
7.34 N
Predefined 11 Phosphorylation
A post-translational modification of proteins in which a serine, threonine or tyrosine residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group.
Phosphorylation reactants Phosphorylation products Acidic 6.9 Acidic 1.2 None H H2PO3 Av: 79.9799 M: 79.9663
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
Y, S, T
Predefined 12 Carbamylation
Carbamylation of lysine and cysteine residues and free N-termini is a nonenzymatic PTM that has been related to protein ageing. It can be artificially introduced during sample preparation with urea, thus affecting studies directed toward in vivo carbamylation. In aqueous solution, urea is in equilibrium with ammonium and isocyanate. The latter can react with primary amines of free N-termini and ε-amine groups of lysines and cysteine sulfhydryls to form carbamyl derivatives.
Carbamylation reactants Carbamylation products None None None CHON Av: 43.0248 M: 43.0058
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
K, C
Predefined 13 Oxidation (methionine)
Protein oxidation is a covalent modification of an amino acid that is induced by reactive oxygen and is often a result of stress or contamination.
Oxidation (methionine) reactants Oxidation (methionine) products None None None O Av: 15.9994 M: 15.9949
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
M
Predefined 14 Acetylation
N-terminal acetylation is one of the most common co-translational covalent modifications of proteins in eukaryotes, and it is crucial for the regulation and function of different proteins. Lit.
Acetylation reactants Acetylation products None None None H C2H3O Av: 42.0368 M: 42.0106
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
K, ^ ^
Glycosylation 15 O-Glycosylation
None None None H2O Av: -18.0153 M: -18.0106
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
S, T
Incomplete 1015 Formylation
In bacteria and organelles, the initiation of protein synthesis is signaled by the formation of formyl-methionyl-tRNA (tRNAfMet). fMet is only used for the initiation of protein synthesis and is thus found only at the N terminus of the protein. Once protein synthesis is accomplished, the formyl group on methionine can be removed by peptide deformylase. Lit.
None None None CO Av: 28.0101 M: 27.9949
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
M, ^ ^(?=M)
Predefined 1016 Amidation (in vivo)
Amidation (in vivo) is a common post-translational modification in peptides and peptide hormones in which the N-Cα bond of a C-terminal glycine is cleaved in two steps by the bifunctional enzyme PAM, resulting in an amidated C-terminus. Lit.
Amidation (in vivo) reactants Amidation (in vivo) products None None None C2H3O2 H Av: -58.0362 M: -58.0055
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
-3 $ (?<=G)$
Incomplete 1018 Methylation (Mono)
Protein methylation, catalyzed by highly specific methyltransferase enzymes, is a relatively common post-translational modification and plays an important role in various biological processes. Monomethylation occurs most frequently at arginine and lysine residues. Lit.
Methylation (Mono) reactants Methylation (Mono) products None None None H CH3 Av: 14.0266 M: 14.0157
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
R, H, K, C, S, T, D, E, ^, $ [KR]
Incomplete 1019 Methylation (Di)
Protein methylation, catalyzed by highly specific methyltransferase enzymes, is a relatively common post-translational modification and plays an important role in various biological processes. Dimethylation occurs most frequently at arginine and lysine residues. Lit.
Methylation (Di) reactants Methylation (Di) products None None None H2 C2H6 Av: 28.0532 M: 28.0313
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
R, K, ^ [KR]
Incomplete 1020 Methylation (Tri)
Protein methylation, catalyzed by highly specific methyltransferase enzymes, is a relatively common post-translational modification and plays an important role in various biological processes. Trimethylation occurs most frequently at lysine residues. Lit.
Methylation (Tri) reactants Methylation (Tri) products None None None H3 C3H9 Av: 42.0799 M: 42.047
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
K, ^ [K]
Incomplete 1021 Sulfation
Sulfation is a common post-translational modification of tyrosine residues in eukaryotes, but has not been observed in yeast and prokaryotes. Sulfation is limited to secretory and transmembrane proteins that have passed the trans-Golgi network, where two membrane-bound tyrosylprotein sulfotransferase enzymes catalyze the transfer of sulfate from adenosine 3’-phosphate 5’-phosphosulfate to the tyrosine phenol. Lit.
Sulfation reactants Sulfation products None None None H SO3H Av: 80.063 M: 79.9568
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
Y
Incomplete 1022 Carboxylation
γ-Carboxylation occurs mainly in proteins related to blood coagulation. Glutamic acid residues are carboxylated by the enzyme glutamyl carboxylase in γ-position in the presence of oxygen and carbon dioxide. Vitamin K is required as a cofactor. Lit.
Carboxylation reactants Carboxylation products Acidic 2.03 None None H CO2H Av: 44.0095 M: 43.9898
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
E
Incomplete 1023 S-Palmitoylation
S-Palmitoylation is a reversible post-translational modifaction, whereby a palmitic acid is covalently attached to cysteine residue of a protein. The reaction is catalyzed by protein palmitoyl acyltransferases. This modification strongly alters the hydrophobicity of the protein. Lit.
S-Palmitoylation reactants S-Palmitoylation products None None None H C16H31O Av: 238.4094 M: 238.2297
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
C
Incomplete 1024 C-Mannosylation
C-Mannosylation is a unique type of protein glycosylation. A C-C bond is formed between the C1 atom of an α-mannose and the C2 atom of the indole ring of a tryptophan residue via mannosyltransferases. Lit.
C-Mannosylation reactants C-Mannosylation products None None None H C6H11O5 Av: 162.1408 M: 162.0528
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
0 W W(?=..W)
Incomplete 1025 mono-ADP-ribosylation
mono-ADP-ribosylation is a common post-translational modification, where an ADP-ribose moiety is transferred from NAD⁺ to the substrate protein under the release of nicotinamide. The transfer of ADP-ribose occurs onto amino acid residues with a nucleophilic oxygen, nitrogen or sulfur. Lit.
mono-ADP-ribosylation reactants mono-ADP-ribosylation products None None None H C15H22N5O13P2 Av: 541.3011 M: 541.0611
λ
/ nm
ε
/ M-1 cm-1
214 20262
240 7836
245 11336
250 14962
255 17675
260 17751
265 15951
270 11843
272 9814
274 7963
276 6238
278 5046
280 3550
282 2612
284 1877
286 1268
288 888
290 558
292 279
294 228
296 127
298 76
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
R, K, N, C, Q, S, T, D, E
Incomplete 1026 N-Myristoylation
N-Myristoylation refers to the covalent linkage of a myristic acid to the N-terminal glycine via an amide bond of many eukaryotic and viral proteins. The reaction is catalyzed by N-myristoyltransferase, is irreversible and affects the hydrophobicity of the protein. Lit.
N-Myristoylation reactants N-Myristoylation products None None None H C14H27O Av: 210.3562 M: 210.1984
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
^ ^(?=G)
Incomplete 1027 Farneslyation
Farnesylation is a subspecies of prenylation in which a 15-carbon isoprenoid lipid is attached to a cysteine residue by farnesyltransferase. Most prenylated proteins contain a CAAX motif at the C-terminus. Lit.
Farneslyation reactants Farneslyation products None None None H C15H25 Av: 204.3516 M: 204.1878
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
C C(?=[AILMFPWYV]{2}[SMAQ])
Incomplete 1028 Geranylgeranylation
Geranylgeranylation is a subspecies of prenylation in which a 20-carbon isoprenoid lipid is attached to a cysteine residue by geranlygeranyltransferase I. Most prenylated proteins contain a CAAX motif at the C-terminus. Lit.
Geranylgeranylation reactants Geranylgeranylation products None None None H C20H33 Av: 272.4688 M: 272.2504
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
C C(?=[AILMFPWYV]{2}L)
Incomplete 1029 Nitration
Nitration is a post-translational modification of mostly tyrosine residues that is caused by oxidation. First, a tyrosine radical is formed by one-electron oxidation followed by a reaction with nitrogen dioxide resulting in 3-nitrotyrosine. Lit.
Nitration reactants Nitration products Acidic 7.25 None None H NO2 Av: 44.9976 M: 44.9851
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 2267
255 2646
260 3308
265 3783
270 4279
272 4321
274 4388
276 4521
278 4588
280 4563
282 4521
284 4642
286 4750
288 4608
290 4421
292 4225
294 3867
296 3496
298 3088
300 2833
302 2583
304 2383
306 2175
308 1921
310 1813
312 1725
314 1658
316 1650
318 1658
320 1679
Y
Incomplete 1030 S-Nitrosylation
S-nitrosylation is a post-translational modification in which a nitric oxide molecule is bound via a reactive thiol group of a cysteine residue. S-nitrosylation has various regulatory roles in bacteria, yeasts, plants and mammalian cells. Lit.
S-Nitrosylation reactants S-Nitrosylation products None None None H NO Av: 28.9982 M: 28.9902
λ
/ nm
ε
/ M-1 cm-1
214 0
240 5848
245 2723
250 1473
255 893
260 893
265 424
270 424
272 424
274 424
276 513
278 603
280 826
282 1004
284 1183
286 1429
288 1652
290 1786
292 2143
294 2500
296 2835
298 3259
300 3728
302 4375
304 4665
306 4978
308 5335
310 5737
312 6094
314 6629
316 6987
318 7321
320 7746
C (?<=[IL].)C(?=.[DE])
Incomplete 1031 Citrullination
Citrulline is a non-proteinogenic amino acid that is produced through post-translational deimination of peptidyl-arginine. Peptidyl-arginine deiminases catalyze the hydrolysis of a guanido group into an urea group.  This modifications affects the formation of hydrogen bonds and therefore protein folding. Lit.
Citrullination reactants Citrullination products None None None NH O Av: 0.9848 M: 0.984
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
R
Predefined 1032 Amidation (in vitro)
Amidation (in vitro) is an artificial modification that can be introduced at the C-terminus of a protein whereby the carboxyl group is replaced by an amide group. The C-terminal amide can be formed by chemical synthesis or by catalysation of carboxypeptidase-Y.
Amidation (in vitro) reactants Amidation (in vitro) products None None None OH NH2 Av: -0.9848 M: -0.984
λ
/ nm
ε
/ M-1 cm-1
214 0
240 0
245 0
250 0
255 0
260 0
265 0
270 0
272 0
274 0
276 0
278 0
280 0
282 0
284 0
286 0
288 0
290 0
292 0
294 0
296 0
298 0
300 0
302 0
304 0
306 0
308 0
310 0
312 0
314 0
316 0
318 0
320 0
-3 $