112806
Pathway
Protein Synthesis: Asparagine
Protein synthesis is an essential life process that builds the important large amino acid macromolecules that function as enzymes, antibodies, and cellular structural components. Although synthesis begins with the transcription of DNA into RNA, this pathway depicts the reactions that occur during translation. Transcribed messenger RNA (mRNA), which contains the genetic code to direct protein synthesis, is transported out of the nucleus and becomes bound to ribosomes in the cytoplasm or endoplasmic reticulum. The amino acids required to assemble polypeptide chains are delivered to the ribosomes using transfer RNA (tRNA). Each tRNA molecule has both a binding site for a specific amino acid and a three-nucleotide sequence called the anticodon that forms three complementary base pairs with an mRNA codon. Charging or loading the appropriate amino acid onto its tRNA is carried out by an aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase. This enzyme catalyzes the esterification of an amino acid to one of all its compatible tRNAs to form an aminoacyl-tRNA. Each of the twenty amino acids has a corresponding aa-tRNA made by a specific aminoacyl-tRNA synthetase. Ribosomes match the anticodons of the charged tRNA molecules with successive codons of the mRNA. After a match is found, the ribosome transfers the amino acid from the matching tRNA onto the growing peptide chain via a reaction termed peptide condensation, and the tRNAs, no longer carrying amino acids, are released.
Protein
PW112910
Center
PathwayVisualizationContext113188
1080
1600
#000099
PathwayVisualization112669
112806
Protein Synthesis: Asparagine
Protein synthesis is an essential life process that builds the important large amino acid macromolecules that function as enzymes, antibodies, and cellular structural components. Although synthesis begins with the transcription of DNA into RNA, this pathway depicts the reactions that occur during translation. Transcribed messenger RNA (mRNA), which contains the genetic code to direct protein synthesis, is transported out of the nucleus and becomes bound to ribosomes in the cytoplasm or endoplasmic reticulum. The amino acids required to assemble polypeptide chains are delivered to the ribosomes using transfer RNA (tRNA). Each tRNA molecule has both a binding site for a specific amino acid and a three-nucleotide sequence called the anticodon that forms three complementary base pairs with an mRNA codon. Charging or loading the appropriate amino acid onto its tRNA is carried out by an aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase. This enzyme catalyzes the esterification of an amino acid to one of all its compatible tRNAs to form an aminoacyl-tRNA. Each of the twenty amino acids has a corresponding aa-tRNA made by a specific aminoacyl-tRNA synthetase. Ribosomes match the anticodons of the charged tRNA molecules with successive codons of the mRNA. After a match is found, the ribosome transfers the amino acid from the matching tRNA onto the growing peptide chain via a reaction termed peptide condensation, and the tRNAs, no longer carrying amino acids, are released.
Protein
1
106363
4
SubPathway
105145
110
Compound
8
277831
12962325
Odintsova TI, Muller EC, Ivanov AV, Egorov TA, Bienert R, Vladimirov SN, Kostka S, Otto A, Wittmann-Liebold B, Karpova GG: Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing. J Protein Chem. 2003 Apr;22(3):249-58.
112806
Pathway
277832
8706699
Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A: Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. Eur J Biochem. 1996 Jul 1;239(1):144-9.
112806
Pathway
1
Cell
CL:0000000
2
Platelet
CL:0000233
5
Hepatocyte
CL:0000182
3
Neuron
CL:0000540
4
Cardiomyocyte
CL:0000746
8
Beta cell
CL:0000639
7
Epithelial Cell
CL:0000066
1
Homo sapiens
9606
Eukaryote
Human
2
Bacteria
2
Prokaryote
Bacteria
3
Escherichia coli
562
Prokaryote
12
Mus musculus
10090
Eukaryote
Mouse
17
Rattus norvegicus
10116
Eukaryote
Rat
19
Schizosaccharomyces pombe
4896
Eukaryote
24
Solanum lycopersicum
4081
Eukaryote
Tomato
4
Arabidopsis thaliana
3702
Eukaryote
Thale cress
18
Saccharomyces cerevisiae
4932
Eukaryote
Yeast
21
Xenopus laevis
8355
Eukaryote
African clawed frog
6
Caenorhabditis elegans
6239
Eukaryote
Roundworm
25
Escherichia coli (strain K12)
83333
Prokaryote
49
Bathymodiolus platifrons
220390
Eukaryote
Deep sea mussel
23
Pseudomonas aeruginosa
287
Prokaryote
60
Nitzschia sp.
0001
Eukaryote
Nitzschia4
5
Bos taurus
9913
Eukaryote
Cattle
10
Drosophila melanogaster
7227
Eukaryote
Fruit fly
51
Picea sitchensis
3332
Eukaryote
Sitka spruce
1
Cytosol
GO:0005829
3
Mitochondrial Matrix
GO:0005759
5
Cytoplasm
GO:0005737
14
Mitochondrial Outer Membrane
GO:0005741
2
Mitochondrion
GO:0005739
15
Nucleus
GO:0005634
4
Peroxisome
GO:0005777
13
Endoplasmic Reticulum
GO:0005783
7
Endoplasmic Reticulum Membrane
GO:0005789
10
Cell Membrane
GO:0005886
27
Peroxisome Membrane
GO:0005778
31
Periplasmic Space
GO:0005620
11
Extracellular Space
GO:0005615
35
Chloroplast
GO:0009507
12
Mitochondrial Inner Membrane
GO:0005743
32
Inner Membrane
GO:0070258
2
Endothelium
BTO:0000393
1
Liver
BTO:0000759
72
9
7
Nervous System
BTO:0001484
18
Pancreas
BTO:0000988
25
Intestine
BTO:0000648
8
Blood Vessel
BTO:0001102
74
11
2
1
1
1
PW_BS000002
4
3
1
1
PW_BS000004
8
5
1
1
PW_BS000008
16
2
1
2
PW_BS000016
22
14
1
1
PW_BS000022
13
1
2
1
PW_BS000013
32
1
15
1
5
PW_BS000032
5
4
1
1
PW_BS000005
39
7
1
1
3
PW_BS000039
3
2
1
1
PW_BS000003
18
13
1
1
PW_BS000018
10
1
7
1
1
PW_BS000010
49
7
1
1
PW_BS000049
14
10
1
PW_BS000014
58
1
14
1
1
PW_BS000058
59
27
1
1
PW_BS000059
27
15
1
PW_BS000027
46
1
1
4
PW_BS000046
29
1
1
1
PW_BS000029
66
18
5
1
8
PW_BS000066
72
5
1
3
PW_BS000072
61
25
1
7
PW_BS000061
51
8
1
PW_BS000051
23
15
1
1
PW_BS000023
31
1
5
1
1
PW_BS000031
91
8
5
1
1
PW_BS000091
54
1
3
1
5
PW_BS000054
89
2
PW_BS000089
26
1
1
1
5
PW_BS000026
7
1
1
PW_BS000007
97
1
5
2
1
PW_BS000097
100
5
2
1
PW_BS000100
104
14
3
1
PW_BS000104
101
5
3
1
PW_BS000101
111
5
12
1
PW_BS000111
112
2
12
1
PW_BS000112
103
3
3
1
PW_BS000103
117
1
3
1
PW_BS000117
118
1
17
1
PW_BS000118
120
3
17
1
PW_BS000120
129
1
5
12
1
PW_BS000129
132
1
12
1
PW_BS000132
133
3
12
1
PW_BS000133
135
5
17
1
PW_BS000135
108
1
3
PW_BS000108
143
1
5
19
1
PW_BS000143
146
5
19
1
PW_BS000146
107
31
3
PW_BS000107
147
1
24
1
PW_BS000147
151
1
4
1
PW_BS000151
155
3
24
1
PW_BS000155
161
3
18
1
PW_BS000161
166
1
1
PW_BS000166
178
3
21
1
PW_BS000178
188
1
18
PW_BS000024
160
1
18
1
PW_BS000160
199
14
18
1
PW_BS000024
205
5
6
1
PW_BS000024
206
2
6
1
PW_BS000024
210
13
18
1
PW_BS000024
213
7
18
1
PW_BS000024
211
10
18
PW_BS000024
198
5
18
1
PW_BS000024
216
4
18
1
PW_BS000024
217
15
18
PW_BS000024
218
15
18
1
PW_BS000024
163
2
18
1
PW_BS000163
222
3
4
1
PW_BS000024
190
11
18
PW_BS000024
225
35
4
1
PW_BS000024
277
1
2
18
PW_BS000024
170
18
PW_BS000170
281
1
25
1
PW_BS000024
164
4
PW_BS000164
285
10
4
1
PW_BS000024
226
4
4
1
PW_BS000024
290
5
49
1
PW_BS000024
223
12
4
1
PW_BS000024
308
10
1
1
PW_BS000024
315
1
23
PW_BS000024
322
1
23
1
PW_BS000024
318
31
23
PW_BS000024
253
5
4
1
PW_BS000024
134
12
12
1
PW_BS000134
329
14
12
1
PW_BS000028
333
1
2
12
PW_BS000028
336
1
12
1
PW_BS000028
332
1
7
12
1
PW_BS000028
350
1
14
12
1
PW_BS000028
128
15
12
1
PW_BS000128
351
15
12
PW_BS000028
353
25
12
7
PW_BS000028
335
27
12
1
PW_BS000028
115
10
12
PW_BS000115
130
13
12
1
PW_BS000130
331
7
12
1
PW_BS000028
334
4
12
1
PW_BS000028
368
3
60
1
PW_BS000028
184
1
2
1
PW_BS000024
119
2
17
1
PW_BS000119
1
1
PW_BS000001
124
1
5
1
PW_BS000124
94
3
PW_BS000094
388
1
6
1
PW_BS000112
109
32
3
PW_BS000109
122
5
5
1
PW_BS000122
406
3
5
1
PW_BS000115
407
2
5
1
PW_BS000115
382
14
5
1
PW_BS000100
412
1
2
5
PW_BS000115
429
1
5
1
PW_BS000115
123
1
7
5
1
PW_BS000123
433
1
14
5
1
PW_BS000115
408
4
5
1
PW_BS000115
410
15
5
1
PW_BS000115
125
13
5
1
PW_BS000125
383
7
5
1
PW_BS000100
405
10
5
PW_BS000115
422
27
5
1
PW_BS000115
435
15
5
PW_BS000115
399
14
17
1
PW_BS000113
446
1
2
17
PW_BS000115
464
1
17
1
PW_BS000115
447
1
7
17
1
PW_BS000115
468
1
14
17
1
PW_BS000115
374
4
17
1
PW_BS000053
444
15
17
1
PW_BS000115
136
13
17
1
PW_BS000136
398
7
17
1
PW_BS000113
376
10
17
PW_BS000053
472
25
17
7
PW_BS000115
375
27
17
1
PW_BS000053
470
15
17
PW_BS000115
297
5
10
1
PW_BS000024
479
3
10
1
PW_BS000115
299
1
10
1
PW_BS000024
481
2
10
1
PW_BS000115
484
14
10
1
PW_BS000115
485
15
10
1
PW_BS000115
300
13
10
1
PW_BS000024
495
7
10
1
PW_BS000115
478
10
10
PW_BS000115
491
27
10
1
PW_BS000115
499
15
10
PW_BS000115
501
3
6
1
PW_BS000115
389
14
6
1
PW_BS000112
516
15
6
1
PW_BS000115
395
13
6
1
PW_BS000113
390
7
6
1
PW_BS000112
209
10
6
PW_BS000024
508
27
6
1
PW_BS000115
517
15
6
PW_BS000115
502
4
6
1
PW_BS000115
249
13
4
1
PW_BS000024
288
14
4
1
PW_BS000024
306
35
51
1
PW_BS000024
17
12
1
1
PW_BS000017
372
10
2
PW_BS000028
384
12
5
1
PW_BS000100
391
12
6
1
PW_BS000112
121
12
17
1
PW_BS000121
105
11
3
PW_BS000105
222
PW_B000222
577
11001
ProteinComplex
1
578
11454
ProteinComplex
1
579
490
ElementCollection
1
225
PW_B000225
589
4
NucleicAcid
1
590
11001
ProteinComplex
1
591
11454
ProteinComplex
1
592
490
ElementCollection
1
414
Adenosine triphosphate
HMDB0000538
Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (PMID: 15490415, 15129319, 14707763, 14696970, 11157473).
56-65-5
C00002
5957
15422
ATP
5742
DB00171
NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O
C10H16N5O13P3
InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid
507.181
506.995745159
-2.05
7
adenosine triphosphate
0
-3
FDB021813
5'-(tetrahydrogen triphosphate) adenosine;5'-atp;Atp;Adenosine 5'-triphosphate;Adenosine 5'-triphosphorate;Adenosine 5'-triphosphoric acid;Adenosine triphosphate;Adenylpyrophosphorate;Adenylpyrophosphoric acid;Adephos;Adetol;Adynol;Atipi;Atriphos;Cardenosine;Fosfobion;Glucobasin;Myotriphos;Phosphobion;Striadyne;Triadenyl;Triphosphaden;Triphosphoric acid adenosine ester;Adenosine-5'-triphosphate;H4atp;Adenosine triphosphoric acid;Adenosine-5'-triphosphoric acid
PW_C000414
ATP
9
2
21
4
60
8
266
16
414
22
478
13
733
32
799
5
934
39
976
3
2105
18
2112
10
2146
49
2156
14
2160
58
2405
59
2434
27
2726
46
2812
29
3029
66
3163
72
3616
61
3617
51
4399
23
4474
31
4768
91
4864
54
5032
89
5035
26
5155
7
5205
97
5215
100
5250
104
5291
101
5313
111
5346
112
5390
103
5406
117
5430
118
5443
120
5542
129
5556
132
5569
133
5603
135
5621
108
5846
143
5854
146
5876
107
5897
147
5924
151
6048
155
6109
161
6230
166
6493
178
6839
188
6870
160
6976
199
7157
205
7184
206
7209
210
7225
213
7229
211
7298
198
7302
216
7390
217
7408
218
7432
163
7481
222
7499
190
8186
225
11847
277
11903
170
12010
281
12039
164
12178
285
12578
226
12691
290
13264
223
15327
308
42326
315
42621
322
42694
318
77028
253
77218
134
77233
329
77468
333
77632
336
78037
332
78041
350
78168
128
78214
351
78240
353
78411
335
78494
115
78850
130
78865
331
78919
334
80028
368
80046
184
80674
119
85629
1
94826
124
113234
94
113282
388
116280
109
119914
122
119992
406
120154
407
120245
382
120362
412
121246
429
121392
123
121397
433
121471
408
121974
410
122065
125
122079
383
122083
405
122402
422
122444
435
122919
399
123009
446
123816
464
123951
447
123956
468
124029
374
124527
444
124616
136
124630
398
124634
376
124943
472
124972
375
125011
470
125304
297
125371
479
125392
299
125515
481
125595
484
126123
485
126220
300
126234
495
126240
478
126547
491
126596
499
126913
501
127123
389
127731
516
127781
395
127796
390
127801
209
128119
508
128167
517
32
Adenosine monophosphate
HMDB0000045
Adenosine monophosphate, also known as 5'-adenylic acid and abbreviated AMP, is a nucleotide that is found in RNA. It is an ester of phosphoric acid with the nucleoside adenosine. AMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase adenine. AMP can be produced during ATP synthesis by the enzyme adenylate kinase. AMP has recently been approved as a 'Bitter Blocker' additive to foodstuffs. When AMP is added to bitter foods or foods with a bitter aftertaste it makes them seem 'sweeter'. This potentially makes lower calorie food products more palatable.
61-19-8
C00020
6083
16027
AMP
5858
DB00131
NC1=C2N=CN([C@@H]3O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]3O)C2=NC=N1
C10H14N5O7P
InChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
UDMBCSSLTHHNCD-KQYNXXCUSA-N
{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}phosphonic acid
347.2212
347.063084339
-2.02
5
adenylate
0
-2
DBMET00485
FDB021806
5'-amp;5'-adenosine monophosphate;5'-adenylate;5'-adenylic acid;Amp;Adenosine 5'-monophosphate;Adenosine 5'-phosphate;Adenosine 5'-phosphorate;Adenosine 5'-phosphoric acid;Adenosine phosphate;Adenosine-5'-monophosphorate;Adenosine-5'-monophosphoric acid;Adenosine-5-monophosphorate;Adenosine-5-monophosphoric acid;Adenosine-monophosphate;Adenosine-phosphate;Adenovite;Adenylate;Adenylic acid;Cardiomone;Lycedan;Muscle adenylate;Muscle adenylic acid;My-b-den;My-beta-den;Phosaden;Phosphaden;Phosphentaside;5'-o-phosphonoadenosine;Adenosine 5'-(dihydrogen phosphate);Adenosine monophosphate;Adenosine-5'p;Adenosini phosphas;Ado5'p;Fosfato de adenosina;Pa;Pado;Phosphate d'adenosine;5'-adenosine monophosphoric acid;Adenosine phosphoric acid;Adenosine 5'-(dihydrogen phosphoric acid);Adenosine 5'-monophosphoric acid;Adenosine monophosphoric acid;Adenosine-5'-monophosphate;Phosphoric acid d'adenosine
PW_C000032
AMP
11
2
34
4
62
8
270
16
734
32
881
22
1189
14
4572
5
4867
54
5033
89
5251
104
5408
117
5423
103
5432
118
5457
120
5558
132
5583
133
5779
101
5795
108
6977
199
7072
188
11789
198
11868
161
11988
151
12003
222
12580
226
12636
31
12694
290
13331
225
42266
3
42646
315
77234
329
77325
111
78392
334
78809
115
79320
112
80399
1
80684
135
80900
7
119916
122
120016
124
120031
406
120246
382
120888
405
121954
408
122920
399
123464
376
124507
374
125306
297
125394
299
125409
479
125596
484
126853
205
126934
388
126949
501
127124
389
127311
209
127711
502
170
Pyrophosphate
HMDB0000250
The anion, the salts, and the esters of pyrophosphoric acid are called pyrophosphates. The pyrophosphate anion is abbreviated PPi and is formed by the hydrolysis of ATP into AMP in cells. This hydrolysis is called pyrophosphorolysis. The pyrophosphate anion has the structure P2O74-, and is an acid anhydride of phosphate. It is unstable in aqueous solution and rapidly hydrolyzes into inorganic phosphate. Pyrophosphate is an osteotoxin (arrests bone development) and an arthritogen (promotes arthritis). It is also a metabotoxin (an endogenously produced metabolite that causes adverse health affects at chronically high levels). Chronically high levels of pyrophosphate are associated with hypophosphatasia. Hypophosphatasia (also called deficiency of alkaline phosphatase or phosphoethanolaminuria) is a rare, and sometimes fatal, metabolic bone disease. Hypophosphatasia is associated with a molecular defect in the gene encoding tissue non-specific alkaline phosphatase (TNSALP). TNSALP is an enzyme that is tethered to the outer surface of osteoblasts and chondrocytes. TNSALP hydrolyzes several substances, including inorganic pyrophosphate (PPi) and pyridoxal 5'-phosphate (PLP), a major form of vitamin B6. When TSNALP is low, inorganic pyrophosphate (PPi) accumulates outside of cells and inhibits the formation of hydroxyapatite, one of the main components of bone, causing rickets in infants and children and osteomalacia (soft bones) in adults. Vitamin B6 must be dephosphorylated by TNSALP before it can cross the cell membrane. Vitamin B6 deficiency in the brain impairs synthesis of neurotransmitters which can cause seizures. In some cases, a build-up of calcium pyrophosphate dihydrate crystals in the joints can cause pseudogout.
14000-31-8
C00013
644102
18361
PPI
559142
DB04160
[O-]P([O-])(=O)OP([O-])([O-])=O
O7P2
InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-4
XPPKVPWEQAFLFU-UHFFFAOYSA-J
(phosphonooxy)phosphonic acid
173.9433
173.911925378
4
pyrophosphoric acid
0
-3
FDB021918
(4-)diphosphoric acid ion;(p2o74-)diphosphate;Diphosphate;Diphosphoric acid;Ppi;Pyrometaphosphate;Pyrophosphate;Pyrophosphate tetraanion;Pyrophosphate(4-) ion;[o3popo3](4-);Diphosphat;P2o7(4-);Pyrophosphat;Pyrophosphate ion;Phosphonato phosphoric acid;Pyrophosphoric acid;Pyrophosphoric acid ion
PW_C000170
Ppi
12
2
35
4
63
8
429
23
735
32
882
22
1217
3
1620
49
2410
59
2815
29
4175
14
4868
54
5034
89
5252
104
5294
101
5409
117
5424
103
5433
118
5458
120
5548
111
5559
132
5584
133
5606
135
5655
108
5879
107
6239
166
6978
199
7073
188
7134
163
7272
160
7312
198
7318
213
8275
151
8283
210
11869
161
12002
222
12041
164
12315
225
12323
249
12512
288
12579
226
12695
290
15219
306
15375
18
34760
17
42561
315
42697
318
77235
329
77317
128
77635
336
78416
335
78928
331
79153
112
79950
134
79958
130
80047
372
80417
170
85630
1
94786
384
94814
125
94819
382
98678
223
110634
391
113270
395
113275
389
115527
136
115532
399
119934
122
120017
124
120032
406
120330
410
120936
407
121261
429
121341
121
121486
383
122407
422
122985
444
123502
119
123831
464
124044
398
124977
375
125324
297
125395
299
125410
479
125597
484
125656
485
125876
481
126552
491
126869
205
126935
388
126950
501
127337
206
128124
508
110
L-Asparagine
HMDB0000168
Asparagine (Asn) is one of the 20 most common natural amino acids on Earth. It has carboxamide as the side chain's functional group. Asparagine is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme. The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. Glutamine donates an ammonium group which reacts with beta-aspartyl-AMP to form asparagine and free AMP. Since the asparagine side chain can make efficient hydrogen bond interactions with the peptide backbone, asparagines are often found near the beginning and end of alpha-helices, and in turn motifs in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions which would otherwise need to be satisfied by the polypeptide backbone. Glutamines have an extra methylene group and have more conformational entropy, and thus are less useful in this regard. Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. A reaction between asparagine and reducing sugars or reactive carbonyls produces acrylamide (acrylic amide) in food when heated to sufficient temperature (i.e. baking). These occur primarily in baked goods such as french fries, potato chips, and roasted coffee. Asparagine was first isolated in 1806 from asparagus juice, in which it is abundant--hence its name--becoming the first amino acid to be isolated. The smell observed in the urine of some individuals after their consumption of asparagus is attributed to a byproduct of the metabolic breakdown of asparagine, asparagine-amino-succinic-acid monoamide. However, some scientists disagree and implicate other substances in the smell, especially methanethiol (Wikipedia).
70-47-3
C00152
6267
17196
ASN
6031
DB00174
N[C@@H](CC(N)=O)C(O)=O
C4H8N2O3
InChI=1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
DCXYFEDJOCDNAF-REOHCLBHSA-N
(2S)-2-amino-3-carbamoylpropanoic acid
132.1179
132.053492132
0.10
3
L-asparagine
0
0
FDB000787
(-)-asparagine;(s)-2,4-diamino-4-oxobutanoate;(s)-2,4-diamino-4-oxobutanoic acid;(s)-asparagine;2-aminosuccinamate;2-aminosuccinamic acid;Agedoite;Altheine;Asn;Asparagine;Asparagine acid;Asparamide;Aspartamate;Aspartamic acid;Aspartic acid amide;Aspartic acid b-amide;Aspartic acid beta amide;B2,4-(s)-diamino-4-oxo-utanoate;B2,4-(s)-diamino-4-oxo-utanoic acid;Crystal vi;L-2,4-diamino-4-oxobutanoate;L-2,4-diamino-4-oxobutanoic acid;L-asparagine;L-aspartamine;L-b-asparagine;L-beta-asparagine;A-aminosuccinamate;A-aminosuccinamic acid;Alpha amminosuccinamate;Alpha amminosuccinamic acid;Alpha-aminosuccinamate;Alpha-aminosuccinamic acid;(2s)-2,4-diamino-4-oxobutanoic acid;(2s)-2-amino-3-carbamoylpropanoic acid;(s)-2-amino-3-carbamoylpropanoic acid;L-2-aminosuccinamic acid;L-asparagin;L-aspartic acid beta-amide;N;(2s)-2,4-diamino-4-oxobutanoate;(2s)-2-amino-3-carbamoylpropanoate;(s)-2-amino-3-carbamoylpropanoate;α-aminosuccinamate;α-aminosuccinamic acid;L-2-aminosuccinamate;L-aspartate b-amide;L-aspartate beta-amide;L-aspartate β-amide;L-aspartic acid b-amide;L-aspartic acid β-amide
PW_C000110
Asn
64
8
5671
107
5672
108
5889
105
12696
290
42417
318
42418
315
77322
111
120039
122
122791
135
125417
297
126957
205
490
mRNA
NucleicAcid
NucleicAcid
PW_EC000490
mRNA
4
L-Asparaginyl-tRNA(Asn)
RNA
PW_NA000004
29265
LATA
69
8
12699
290
77529
111
120064
122
122816
135
125441
297
126980
205
3036
4
12
8
true
1249
0
14
150
regular
150
70
3
tRNA(Asn)
RNA
PW_NA000003
29172
TRNAASN
68
8
12698
290
77528
111
120063
122
122815
135
125440
297
126979
205
8096
60S ribosomal protein L3
P39023
The L3 protein is a component of the large subunit of cytoplasmic ribosomes.
RPL3
1
133190
8
8109
60S ribosomal protein L4
P36578
RPL4
1
133191
8
8111
60S ribosomal protein L5
P46777
Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA.
RPL5
1
133192
8
8112
60S ribosomal protein L6
Q02878
Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I.
RPL6
1
133193
8
8114
60S ribosomal protein L7a
P62424
RPL7A
1
133194
8
8113
60S ribosomal protein L7
P18124
Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.
RPL7
1
133195
8
8115
60S ribosomal protein L8
P62917
RPL8
1
133196
8
8116
60S ribosomal protein L9
P32969
RPL9
1
133197
8
8077
60S ribosomal protein L10a
P62906
RPL10A
1
133198
8
8076
60S ribosomal protein L10
P27635
RPL10
1
133199
8
8078
60S ribosomal protein L11
P62913
Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity).
RPL11
1
133200
8
8079
60S ribosomal protein L12
P30050
Binds directly to 26S ribosomal RNA.
RPL12
1
133201
8
8081
60S ribosomal protein L13a
P40429
Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA.
RPL13A
1
133202
8
8080
60S ribosomal protein L13
P26373
RPL13
1
133203
8
8082
60S ribosomal protein L14
P50914
RPL14
1
133204
8
8083
60S ribosomal protein L15
P61313
RPL15
1
133205
8
8084
60S ribosomal protein L17
P18621
RPL17
1
133206
8
8086
60S ribosomal protein L18a
Q02543
RPL18A
1
133207
8
8085
60S ribosomal protein L18
Q07020
RPL18
1
133208
8
8087
60S ribosomal protein L19
P84098
RPL19
1
133209
8
8088
60S ribosomal protein L21
P46778
RPL21
1
133210
8
4811
60S ribosomal protein L22
P35268
HMDBP10729
RPL22
1p36.31
BC035566
1
133211
8
8090
60S ribosomal protein L23a
P62750
This protein binds to a specific region on the 26S rRNA.
RPL23A
1
133212
8
8089
60S ribosomal protein L23
P62829
RPL23
1
133213
8
8091
60S ribosomal protein L24
P83731
RPL24
1
133214
8
8092
60S ribosomal protein L26
P61254
RPL26
1
133215
8
8094
60S ribosomal protein L27a
P46776
RPL27A
1
133216
8
8093
60S ribosomal protein L27
P61353
RPL27
1
133217
8
8095
60S ribosomal protein L28
P46779
RPL28
1
133218
8
4810
60S ribosomal protein L29
P47914
HMDBP10728
RPL29
3p21.3-p21.2
AK311884
1
133219
8
8097
60S ribosomal protein L30
P62888
RPL30
1
133220
8
8098
60S ribosomal protein L31
P62899
RPL31
1
133221
8
8099
60S ribosomal protein L32
P62910
RPL32
1
133222
8
8100
60S ribosomal protein L34
P49207
RPL34
1
133223
8
8102
60S ribosomal protein L35a
P18077
Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site.
RPL35A
1
133224
8
8101
60S ribosomal protein L35
P42766
RPL35
1
133225
8
8104
60S ribosomal protein L36a
P83881
RPL36A
1
133226
8
8103
60S ribosomal protein L36
Q9Y3U8
RPL36
1
133227
8
8106
60S ribosomal protein L37a
P61513
RPL37A
1
133228
8
8105
60S ribosomal protein L37
P61927
Binds to the 23S rRNA.
RPL37
1
133229
8
8107
60S ribosomal protein L38
P63173
RPL38
1
133230
8
8108
60S ribosomal protein L39
P62891
RPL39
1
133231
8
8120
Ubiquitin-60S ribosomal protein L40
P62987
Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
UBA52
1
133232
8
8110
60S ribosomal protein L41
P62945
Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII.
RPL41
1
133233
8
8117
60S acidic ribosomal protein P0
P05388
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
RPLP0
1
133234
8
8118
60S acidic ribosomal protein P1
P05386
Plays an important role in the elongation step of protein synthesis.
RPLP1
1
133235
8
8119
60S acidic ribosomal protein P2
P05387
Plays an important role in the elongation step of protein synthesis.
RPLP2
1
133236
8
8043
40S ribosomal protein S2
P15880
RPS2
1
133237
8
8053
40S ribosomal protein S3
P23396
Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).
RPS3
1
4.2.99.18
133238
8
8054
40S ribosomal protein S3a
P61247
May play a role during erythropoiesis through regulation of transcription factor DDIT3.
RPS3A
1
133239
8
8055
40S ribosomal protein S4, X isoform
P62701
RPS4X
1
133240
8
8056
40S ribosomal protein S5
P46782
RPS5
1
133241
8
8057
40S ribosomal protein S6
P62753
May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.
RPS6
1
133242
8
8058
40S ribosomal protein S7
P62081
Required for rRNA maturation.
RPS7
1
133243
8
8059
40S ribosomal protein S8
P62241
RPS8
1
133244
8
8060
40S ribosomal protein S9
P46781
RPS9
1
133245
8
8032
40S ribosomal protein S10
P46783
Component of the 40S ribosomal subunit.
RPS10
1
133246
8
8033
40S ribosomal protein S11
P62280
RPS11
1
133247
8
8034
40S ribosomal protein S12
P25398
RPS12
1
133248
8
8035
40S ribosomal protein S13
P62277
RPS13
1
133249
8
8036
40S ribosomal protein S14
P62263
RPS14
1
133250
8
8037
40S ribosomal protein S15
P62841
RPS15
1
133251
8
8038
40S ribosomal protein S15a
P62244
RPS15A
1
133252
8
8039
40S ribosomal protein S16
P62249
RPS16
1
133253
8
8040
40S ribosomal protein S17
P08708
RPS17
1
133254
8
8041
40S ribosomal protein S18
P62269
Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.
RPS18
1
133255
8
8042
40S ribosomal protein S19
P39019
Required for pre-rRNA processing and maturation of 40S ribosomal subunits.
RPS19
1
133256
8
8044
40S ribosomal protein S20
P60866
RPS20
1
133257
8
8045
40S ribosomal protein S21
P63220
RPS21
1
133258
8
8046
40S ribosomal protein S23
P62266
RPS23
1
133259
8
8047
40S ribosomal protein S24
P62847
Required for processing of pre-rRNA and maturation of 40S ribosomal subunits.
RPS24
1
133260
8
8048
40S ribosomal protein S25
P62851
RPS25
1
133261
8
8049
40S ribosomal protein S26
P62854
RPS26
1
133262
8
3391
40S ribosomal protein S27
P42677
HMDBP08171
RPS27
1q21
CH471121
1
133263
8
8051
40S ribosomal protein S28
P62857
RPS28
1
133264
8
8052
40S ribosomal protein S29
P62273
RPS29
1
133265
8
8031
40S ribosomal protein S30
P62861
FAU
1
133266
8
8061
40S ribosomal protein SA
P08865
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria.
RPSA
1
133267
8
8840
Receptor of activated protein C kinase 1
P63244
Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158).
RACK1
1
133268
8
578
Asparagine--tRNA ligase, cytoplasmic
O43776
HMDBP00611
NARS
18q21.31
D84273
1
6.1.1.22
70
8
11001
Large 60S Ribosomal Subunit
1
PW_P011001
19588
8096
20243
8109
20244
8111
20252
8112
20253
8114
20254
8113
20255
8115
20256
8116
20257
8077
20258
8076
20259
8078
20260
8079
20261
8081
20262
8080
20263
8082
20264
8083
20265
8084
20266
8086
20267
8085
20268
8087
20269
8088
20281
4811
20282
8090
20283
8089
20287
8091
20289
8092
20290
8094
20306
8093
20307
8095
20308
4810
20309
8097
20310
8098
20311
8099
20312
8100
20313
8102
20314
8101
20315
8104
20316
8103
20317
8106
20318
8105
20333
8107
20334
8108
20335
8120
20336
8110
20337
8117
20338
8118
20339
8119
11454
Small 40S Ribosomal Subunit
1
PW_P011454
20347
8043
20349
8053
20350
8054
20351
8055
20352
8056
20353
8057
20354
8058
20355
8059
20356
8060
20357
8032
20358
8033
20359
8034
20360
8035
20361
8036
20362
8037
20363
8038
20395
8039
20396
8040
20397
8041
20398
8042
20399
8044
20400
8045
20401
8046
20402
8047
20403
8048
20404
8049
20405
3391
20406
8051
20407
8052
20408
8031
20409
8061
20410
8840
10
Asparagine--tRNA ligase, cytoplasmic
1
PW_P000010
11
578
1
67
8
178634
PW_R178634
Right
674153
4
1
NucleicAcid
false
674154
222
1
Bound
false
674155
225
1
Bound
false
10
false
PW_R000010
Both
43
414
1
Compound
true
44
110
1
Compound
false
45
3
1
NucleicAcid
true
46
32
1
Compound
true
47
170
1
Compound
true
48
4
1
NucleicAcid
false
11
10
6.1.1.22
1010
222
8
112669
281
12180
3568426
1467
781740
3568427
1468
781741
3568428
1011
225
8
112669
282
12181
3568430
9
3036
3568431
1469
781742
3568432
1470
781743
3568433
2626223
414
8
42
false
335
702
10
regular
50
30
2626225
32
8
44
false
645
700
10
regular
50
30
2626226
170
8
45
false
638
465
10
regular
63
43
2649674
110
8
3
false
295
411
10
regular
100
100
12180
490
37
8
true
769
0
12
regular
100
90
12181
490
37
8
true
1159
0
12
regular
100
90
3034
3
96
8
false
225
577
14
120
nucleic_acid
regular
120
115
3035
4
96
8
false
689
580
14
120
nucleic_acid
regular
120
115
3036
4
12
8
true
1249
0
14
150
regular
150
70
900298
8096
8
2
true
629
0
8
subunit
regular
150
70
900299
8109
8
2
true
629
60
8
subunit
regular
150
70
900300
8111
8
2
true
629
120
8
subunit
regular
150
70
900301
8112
8
2
true
629
180
8
subunit
regular
150
70
900302
8114
8
2
true
629
240
8
subunit
regular
150
70
900303
8113
8
2
true
629
300
8
subunit
regular
150
70
900304
8115
8
2
true
629
360
8
subunit
regular
150
70
900305
8116
8
2
true
629
420
8
subunit
regular
150
70
900306
8077
8
2
true
629
480
8
subunit
regular
150
70
900307
8076
8
2
true
629
540
8
subunit
regular
150
70
900308
8078
8
2
true
629
600
8
subunit
regular
150
70
900309
8079
8
2
true
629
660
8
subunit
regular
150
70
900310
8081
8
2
true
629
720
8
subunit
regular
150
70
900311
8080
8
2
true
629
780
8
subunit
regular
150
70
900312
8082
8
2
true
629
840
8
subunit
regular
150
70
900313
8083
8
2
true
629
900
8
subunit
regular
150
70
900314
8084
8
2
true
629
960
8
subunit
regular
150
70
900315
8086
8
2
true
629
1020
8
subunit
regular
150
70
900316
8085
8
2
true
629
1080
8
subunit
regular
150
70
900317
8087
8
2
true
629
1140
8
subunit
regular
150
70
900318
8088
8
2
true
629
1200
8
subunit
regular
150
70
900319
4811
8
2
true
629
1260
8
subunit
regular
150
70
900320
8090
8
2
true
629
1320
8
subunit
regular
150
70
900321
8089
8
2
true
629
1380
8
subunit
regular
150
70
900322
8091
8
2
true
629
1440
8
subunit
regular
150
70
900323
8092
8
2
true
629
1500
8
subunit
regular
150
70
900324
8094
8
2
true
629
1560
8
subunit
regular
150
70
900325
8093
8
2
true
629
1620
8
subunit
regular
150
70
900326
8095
8
2
true
629
1680
8
subunit
regular
150
70
900327
4810
8
2
true
629
1740
8
subunit
regular
150
70
900328
8097
8
2
true
629
1800
8
subunit
regular
150
70
900329
8098
8
2
true
629
1860
8
subunit
regular
150
70
900330
8099
8
2
true
629
1920
8
subunit
regular
150
70
900331
8100
8
2
true
629
1980
8
subunit
regular
150
70
900332
8102
8
2
true
629
2040
8
subunit
regular
150
70
900333
8101
8
2
true
629
2100
8
subunit
regular
150
70
900334
8104
8
2
true
629
2160
8
subunit
regular
150
70
900335
8103
8
2
true
629
2220
8
subunit
regular
150
70
900336
8106
8
2
true
629
2280
8
subunit
regular
150
70
900337
8105
8
2
true
629
2340
8
subunit
regular
150
70
900338
8107
8
2
true
629
2400
8
subunit
regular
150
70
900339
8108
8
2
true
629
2460
8
subunit
regular
150
70
900340
8120
8
2
true
629
2520
8
subunit
regular
150
70
900341
8110
8
2
true
629
2580
8
subunit
regular
150
70
900342
8117
8
2
true
629
2640
8
subunit
regular
150
70
900343
8118
8
2
true
629
2700
8
subunit
regular
150
70
900344
8119
8
2
true
629
2760
8
subunit
regular
150
70
900345
8043
8
2
true
629
2820
8
subunit
regular
150
70
900346
8053
8
2
true
629
2880
8
subunit
regular
150
70
900347
8054
8
2
true
629
2940
8
subunit
regular
150
70
900348
8055
8
2
true
629
3000
8
subunit
regular
150
70
900349
8056
8
2
true
629
3060
8
subunit
regular
150
70
900350
8057
8
2
true
629
3120
8
subunit
regular
150
70
900351
8058
8
2
true
629
3180
8
subunit
regular
150
70
900352
8059
8
2
true
629
3240
8
subunit
regular
150
70
900353
8060
8
2
true
629
3300
8
subunit
regular
150
70
900354
8032
8
2
true
629
3360
8
subunit
regular
150
70
900355
8033
8
2
true
629
3420
8
subunit
regular
150
70
900356
8034
8
2
true
629
3480
8
subunit
regular
150
70
900357
8035
8
2
true
629
3540
8
subunit
regular
150
70
900358
8036
8
2
true
629
3600
8
subunit
regular
150
70
900359
8037
8
2
true
629
3660
8
subunit
regular
150
70
900360
8038
8
2
true
629
3720
8
subunit
regular
150
70
900361
8039
8
2
true
629
3780
8
subunit
regular
150
70
900362
8040
8
2
true
629
3840
8
subunit
regular
150
70
900363
8041
8
2
true
629
3900
8
subunit
regular
150
70
900364
8042
8
2
true
629
3960
8
subunit
regular
150
70
900365
8044
8
2
true
629
4020
8
subunit
regular
150
70
900366
8045
8
2
true
629
4080
8
subunit
regular
150
70
900367
8046
8
2
true
629
4140
8
subunit
regular
150
70
900368
8047
8
2
true
629
4200
8
subunit
regular
150
70
900369
8048
8
2
true
629
4260
8
subunit
regular
150
70
900370
8049
8
2
true
629
4320
8
subunit
regular
150
70
900371
3391
8
2
true
629
4380
8
subunit
regular
150
70
900372
8051
8
2
true
629
4440
8
subunit
regular
150
70
900373
8052
8
2
true
629
4500
8
subunit
regular
150
70
900374
8031
8
2
true
629
4560
8
subunit
regular
150
70
900375
8061
8
2
true
629
4620
8
subunit
regular
150
70
900376
8840
8
2
true
629
4680
8
subunit
regular
150
70
900377
8096
8
188
false
1030
596
2
none
regular
300
140
900378
8109
8
2
true
1019
60
8
subunit
regular
150
70
900379
8111
8
2
true
1019
120
8
subunit
regular
150
70
900380
8112
8
2
true
1019
180
8
subunit
regular
150
70
900381
8114
8
2
true
1019
240
8
subunit
regular
150
70
900382
8113
8
2
true
1019
300
8
subunit
regular
150
70
900383
8115
8
2
true
1019
360
8
subunit
regular
150
70
900384
8116
8
2
true
1019
420
8
subunit
regular
150
70
900385
8077
8
2
true
1019
480
8
subunit
regular
150
70
900386
8076
8
2
true
1019
540
8
subunit
regular
150
70
900387
8078
8
2
true
1019
600
8
subunit
regular
150
70
900388
8079
8
2
true
1019
660
8
subunit
regular
150
70
900389
8081
8
2
true
1019
720
8
subunit
regular
150
70
900390
8080
8
2
true
1019
780
8
subunit
regular
150
70
900391
8082
8
2
true
1019
840
8
subunit
regular
150
70
900392
8083
8
2
true
1019
900
8
subunit
regular
150
70
900393
8084
8
2
true
1019
960
8
subunit
regular
150
70
900394
8086
8
2
true
1019
1020
8
subunit
regular
150
70
900395
8085
8
2
true
1019
1080
8
subunit
regular
150
70
900396
8087
8
2
true
1019
1140
8
subunit
regular
150
70
900397
8088
8
2
true
1019
1200
8
subunit
regular
150
70
900398
4811
8
2
true
1019
1260
8
subunit
regular
150
70
900399
8090
8
2
true
1019
1320
8
subunit
regular
150
70
900400
8089
8
2
true
1019
1380
8
subunit
regular
150
70
900401
8091
8
2
true
1019
1440
8
subunit
regular
150
70
900402
8092
8
2
true
1019
1500
8
subunit
regular
150
70
900403
8094
8
2
true
1019
1560
8
subunit
regular
150
70
900404
8093
8
2
true
1019
1620
8
subunit
regular
150
70
900405
8095
8
2
true
1019
1680
8
subunit
regular
150
70
900406
4810
8
2
true
1019
1740
8
subunit
regular
150
70
900407
8097
8
2
true
1019
1800
8
subunit
regular
150
70
900408
8098
8
2
true
1019
1860
8
subunit
regular
150
70
900409
8099
8
2
true
1019
1920
8
subunit
regular
150
70
900410
8100
8
2
true
1019
1980
8
subunit
regular
150
70
900411
8102
8
2
true
1019
2040
8
subunit
regular
150
70
900412
8101
8
2
true
1019
2100
8
subunit
regular
150
70
900413
8104
8
2
true
1019
2160
8
subunit
regular
150
70
900414
8103
8
2
true
1019
2220
8
subunit
regular
150
70
900415
8106
8
2
true
1019
2280
8
subunit
regular
150
70
900416
8105
8
2
true
1019
2340
8
subunit
regular
150
70
900417
8107
8
2
true
1019
2400
8
subunit
regular
150
70
900418
8108
8
2
true
1019
2460
8
subunit
regular
150
70
900419
8120
8
2
true
1019
2520
8
subunit
regular
150
70
900420
8110
8
2
true
1019
2580
8
subunit
regular
150
70
900421
8117
8
2
true
1019
2640
8
subunit
regular
150
70
900422
8118
8
2
true
1019
2700
8
subunit
regular
150
70
900423
8119
8
2
true
1019
2760
8
subunit
regular
150
70
900424
8043
8
186
false
1050
766
2
none
regular
150
70
900425
8053
8
186
false
1175
766
2
none
regular
150
70
900426
8054
8
2
true
1019
2940
8
subunit
regular
150
70
900427
8055
8
2
true
1019
3000
8
subunit
regular
150
70
900428
8056
8
2
true
1019
3060
8
subunit
regular
150
70
900429
8057
8
2
true
1019
3120
8
subunit
regular
150
70
900430
8058
8
2
true
1019
3180
8
subunit
regular
150
70
900431
8059
8
2
true
1019
3240
8
subunit
regular
150
70
900432
8060
8
2
true
1019
3300
8
subunit
regular
150
70
900433
8032
8
2
true
1019
3360
8
subunit
regular
150
70
900434
8033
8
2
true
1019
3420
8
subunit
regular
150
70
900435
8034
8
2
true
1019
3480
8
subunit
regular
150
70
900436
8035
8
2
true
1019
3540
8
subunit
regular
150
70
900437
8036
8
2
true
1019
3600
8
subunit
regular
150
70
900438
8037
8
2
true
1019
3660
8
subunit
regular
150
70
900439
8038
8
2
true
1019
3720
8
subunit
regular
150
70
900440
8039
8
2
true
1019
3780
8
subunit
regular
150
70
900441
8040
8
2
true
1019
3840
8
subunit
regular
150
70
900442
8041
8
2
true
1019
3900
8
subunit
regular
150
70
900443
8042
8
2
true
1019
3960
8
subunit
regular
150
70
900444
8044
8
2
true
1019
4020
8
subunit
regular
150
70
900445
8045
8
2
true
1019
4080
8
subunit
regular
150
70
900446
8046
8
2
true
1019
4140
8
subunit
regular
150
70
900447
8047
8
2
true
1019
4200
8
subunit
regular
150
70
900448
8048
8
2
true
1019
4260
8
subunit
regular
150
70
900449
8049
8
2
true
1019
4320
8
subunit
regular
150
70
900450
3391
8
2
true
1019
4380
8
subunit
regular
150
70
900451
8051
8
2
true
1019
4440
8
subunit
regular
150
70
900452
8052
8
2
true
1019
4500
8
subunit
regular
150
70
900453
8031
8
2
true
1019
4560
8
subunit
regular
150
70
900454
8061
8
2
true
1019
4620
8
subunit
regular
150
70
900455
8840
8
2
true
1019
4680
8
subunit
regular
150
70
914864
578
8
2
false
447
574
8
subunit
regular
150
70
781740
11001
112669
8
897157
900298
897158
900299
897159
900300
897160
900301
897161
900302
897162
900303
897163
900304
897164
900305
897165
900306
897166
900307
897167
900308
897168
900309
897169
900310
897170
900311
897171
900312
897172
900313
897173
900314
897174
900315
897175
900316
897176
900317
897177
900318
897178
900319
897179
900320
897180
900321
897181
900322
897182
900323
897183
900324
897184
900325
897185
900326
897186
900327
897187
900328
897188
900329
897189
900330
897190
900331
897191
900332
897192
900333
897193
900334
897194
900335
897195
900336
897196
900337
897197
900338
897198
900339
897199
900340
897200
900341
897201
900342
897202
900343
897203
900344
781741
11454
112669
8
897204
900345
897205
900346
897206
900347
897207
900348
897208
900349
897209
900350
897210
900351
897211
900352
897212
900353
897213
900354
897214
900355
897215
900356
897216
900357
897217
900358
897218
900359
897219
900360
897220
900361
897221
900362
897222
900363
897223
900364
897224
900365
897225
900366
897226
900367
897227
900368
897228
900369
897229
900370
897230
900371
897231
900372
897232
900373
897233
900374
897234
900375
897235
900376
781742
11001
112669
8
897236
900377
897237
900378
897238
900379
897239
900380
897240
900381
897241
900382
897242
900383
897243
900384
897244
900385
897245
900386
897246
900387
897247
900388
897248
900389
897249
900390
897250
900391
897251
900392
897252
900393
897253
900394
897254
900395
897255
900396
897256
900397
897257
900398
897258
900399
897259
900400
897260
900401
897261
900402
897262
900403
897263
900404
897264
900405
897265
900406
897266
900407
897267
900408
897268
900409
897269
900410
897270
900411
897271
900412
897272
900413
897273
900414
897274
900415
897275
900416
897276
900417
897277
900418
897278
900419
897279
900420
897280
900421
897281
900422
897282
900423
781743
11454
112669
8
897283
900424
897284
900425
897285
900426
897286
900427
897287
900428
897288
900429
897289
900430
897290
900431
897291
900432
897292
900433
897293
900434
897294
900435
897295
900436
897296
900437
897297
900438
897298
900439
897299
900440
897300
900441
897301
900442
897302
900443
897303
900444
897304
900445
897305
900446
897306
900447
897307
900448
897308
900449
897309
900450
897310
900451
897311
900452
897312
900453
897313
900454
897314
900455
790237
10
112669
8
911378
914864
3568406
M100 2100 L100 2150 L150 2100 z
10
true
18
3568425
M805 609 C918 649 969 670 1149 740
5
false
18
true
M 888.9749045598433 581.96644186147 L 901 573 L 887.2222858463324 567.0691827966269
false
3568426
M764 -5 L764 45 L814 -5 z
10
true
18
3568427
M310 309 L310 359 L360 309 z
10
true
18
3568428
M310 3129 L310 3179 L360 3129 z
10
true
18
3568429
M869 50 C899 50 949 -588.75 979 -588.75
5
true
18
3568430
M1154 -5 L1154 45 L1204 -5 z
10
true
18
3568431
M1244 -5 L1244 45 L1294 -5 z
10
true
18
3568432
M310 699 L310 749 L360 699 z
10
true
18
3568433
M310 3519 L310 3569 L360 3519 z
10
true
18
3568434
M1249 35 C1219 35 1009 -588.75 979 -588.75
5
true
18
true
M 340.94685504416486 384.261556296296 L 326 383 L 332.38088772118584 396.5751343230783
false
3606198
M345 411 C345 381 345 340 345 310
5
false
18
true
M 67.5 283.0096189432334 L 75 296 L 82.5 283.0096189432334
false
3606199
M385 717 C390 631 417 609 447 609
5
false
18
true
M 25.946855044164835 185.26155629629605 L 11 184 L 17.380887721185843 197.57513432307834
false
3606200
M395 461 C396 572 417 609 447 609
5
false
18
true
M 25.946855044164835 185.26155629629605 L 11 184 L 17.380887721185843 197.57513432307834
false
3606201
M645 715 C643 647 627 609 597 609
5
false
18
true
M 25.946855044164835 185.26155629629605 L 11 184 L 17.380887721185843 197.57513432307834
false
3606202
M638 486.5 C637 568.5 627 609 597 609
5
false
18
true
M 25.946855044164835 185.26155629629605 L 11 184 L 17.380887721185843 197.57513432307834
false
3606203
M340 607 C370 607 417 609 447 609
5
false
18
true
M 25.946855044164835 185.26155629629605 L 11 184 L 17.380887721185843 197.57513432307834
false
3606204
M694 610 C664 610 627 609 597 609
5
false
18
true
M 25.946855044164835 185.26155629629605 L 11 184 L 17.380887721185843 197.57513432307834
false
781353
112669
178634
8
689
1010
3568429
Left
690
1011
3568434
Right
939
3035
3568425
Left
788435
112669
10
8
3192360
2626223
3606199
Left
3192361
2649674
3606200
Left
3192362
2626225
3606201
Right
3192363
2626226
3606202
Right
1188
3034
3606203
Left
1189
3035
3606204
Right
745188
11
790237
107392
106363
112669
14
false
270
240
16
regular
104158
2649674
3606198
Right
183525
685
172
0.4
0.4
0
1
42
1785
1645
366908
M128 226.5 C128 176.5 178 126.5 228 126.5 C576 126.5 1028 126.5 1376 126.5 C1426 126.5 1476 176.5 1476 226.5 C1476 419.5 1476 669.5 1476 862.5 C1476 912.5 1426 962.5 1376 962.5 C1028 962.5 576 962.5 228 962.5 C178 962.5 128 912.5 128 862.5 C128 669.5 128 419.5 128 226.5
1
true
6
0.0
0.0
443210
15
mRNA
595
746
20
1.3
1.3
160
15
443211
15
Polypeptide Chain
885
442
20
1.3
1.3
160
15
443212
235
Translation
1021
799
20
1.6
1.6
200
15
443213
15
Ribosome
1242
580
20
1.3
1.3
160
15
443214
15
Cytoplasm
1207
173
20
1.3
1.3
160
15