P41250 · GARS_HUMAN
- ProteinGlycine--tRNA ligase
- GeneGARS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids739 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP) (PubMed:17544401, PubMed:24898252, PubMed:28675565).
Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (PubMed:19710017).
Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (PubMed:19710017).
Miscellaneous
Human GlyRS uses direct ATP condensation to synthesize Ap4A, a unique amino acid-independent mechanism, in contrast to the classical amino acid-dependent mechanism for synthesis of Ap4A by a tRNA synthetase, that involves the generation of an enzyme-bound aminoacyl-AMP which is then attacked by ATP to form Ap4A.
Catalytic activity
- ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)This reaction proceeds in the forward direction.
- 2 ATP + H+ = diphosphate + P1,P4-bis(5'-adenosyl) tetraphosphateThis reaction proceeds in the forward direction.
Activity regulation
Ap4A synthesis is inhibited by tRNA, via the disruption of the second ATP-binding site by direct blocking and/or by tRNA-induced conformational change.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.3 μM | tRNA(Gly(GCC)) | |||||
15 μM | glycine | |||||
0.74 μM | tRNA(Gly) |
kcat is 0.049 sec-1 for aminoacylation of tRNA(Gly).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 299 | glycine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 331-333 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RNE | ||||||
Binding site | 342-343 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RV | ||||||
Binding site | 350 | glycine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 457-458 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EI | ||||||
Binding site | 576-578 | glycine (UniProtKB | ChEBI) | ||||
Sequence: EPS | ||||||
Binding site | 583 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | secretory granule | |
Molecular Function | ATP binding | |
Molecular Function | ATP:ATP adenylyltransferase activity | |
Molecular Function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity | |
Molecular Function | glycine-tRNA ligase activity | |
Molecular Function | identical protein binding | |
Molecular Function | protein dimerization activity | |
Biological Process | diadenosine tetraphosphate biosynthetic process | |
Biological Process | mitochondrial glycyl-tRNA aminoacylation | |
Biological Process | tRNA aminoacylation for protein translation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP41250
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In transfected COS7 cells, not detected in mitochondria, nor in Golgi apparatus (PubMed:17035524).
Secreted by motor neuron, possibly through the exosome pathway (By similarity).
Secreted by motor neuron, possibly through the exosome pathway (By similarity).
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Charcot-Marie-Tooth disease, axonal, 2D (CMT2D)
- Note
- DescriptionA dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
- See alsoMIM:601472
Natural variants in CMT2D
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073187 | 111 | A>V | in CMT2D; shows a reduction in aminoacylation activity; dbSNP:rs370531212 | |
VAR_018718 | 125 | E>G | in CMT2D; phenotype overlapping with HMND5; complements the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly binds to NRP1 and competes with VEGFA for NRP1-binding; displays slightly elevated aminoacylation activity over wild-type; dbSNP:rs137852645 | |
VAR_073188 | 200 | D>N | in CMT2D and HMND5; shows a large reduction in aminoacylation activity; dbSNP:rs1554337369 | |
VAR_074016 | 200 | D>Y | in CMT2D; dbSNP:rs1554337369 | |
VAR_073189 | 265 | S>F | in CMT2D and HMND5; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules; dbSNP:rs1554337974 | |
VAR_085141 | 265 | S>Y | in CMT2D; uncertain significance; dbSNP:rs1554337974 | |
VAR_074017 | 292 | M>R | in CMT2D; dbSNP:rs1064795123 | |
VAR_018720 | 294 | G>R | in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability; contrary to the wild-type protein, strongly interacts with NRP1; dbSNP:rs137852643 | |
VAR_073190 | 298 | P>L | in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; dbSNP:rs137852648 | |
VAR_073191 | 334 | I>F | in CMT2D; uncertain significance; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; dbSNP:rs1554338260 | |
VAR_073193 | 554 | D>N | in CMT2D; demonstrates no change in subcellular location pattern; dbSNP:rs137852647 | |
VAR_073195 | 652 | G>A | in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; dbSNP:rs747080824 |
Neuronopathy, distal hereditary motor, autosomal dominant 5 (HMND5)
- Note
- DescriptionA form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.
- See alsoMIM:600794
Natural variants in HMND5
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_018719 | 183 | L>P | in HMND5; does not complement the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly interacts with NRP1; dbSNP:rs137852644 | |
VAR_073188 | 200 | D>N | in CMT2D and HMND5; shows a large reduction in aminoacylation activity; dbSNP:rs1554337369 | |
VAR_073189 | 265 | S>F | in CMT2D and HMND5; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules; dbSNP:rs1554337974 | |
VAR_073192 | 472 | H>R | in HMND5; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast; dbSNP:rs1060502838 | |
VAR_018721 | 580 | G>R | in HMND5; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity; dbSNP:rs137852646 | |
VAR_079829 | 598 | G>A | in HMND5; uncertain significance; dbSNP:rs766280100 |
Spinal muscular atrophy, infantile, James type (SMAJI)
- Note
- DescriptionAn autosomal dominant form of spinal muscular atrophy, a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAJI is a severe disease characterized by hypotonia manifesting in the first weeks or months of life, delayed motor development, motor regression, and muscle weakness and atrophy primarily affecting distal muscles. Additional variable features include feeding difficulties, poor overall growth, foot deformities, kyphosis, hyperlordosis, scoliosis, vocal cord dysfunction, and respiratory insufficiency.
- See alsoMIM:619042
Natural variants in SMAJI
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_085142 | 334 | I>N | in SMAJI; loss of function; based on yeast complementation assay; dbSNP:rs1554338262 | |
VAR_085143 | 652 | G>R | in SMAJI; dbSNP:rs1783251037 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_054865 | 42 | in dbSNP:rs1049402 | |||
Sequence: P → A | ||||||
Natural variant | VAR_073187 | 111 | in CMT2D; shows a reduction in aminoacylation activity; dbSNP:rs370531212 | |||
Sequence: A → V | ||||||
Mutagenesis | 121 | Decrease in catalytic activity by about 10-fold. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_018718 | 125 | in CMT2D; phenotype overlapping with HMND5; complements the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly binds to NRP1 and competes with VEGFA for NRP1-binding; displays slightly elevated aminoacylation activity over wild-type; dbSNP:rs137852645 | |||
Sequence: E → G | ||||||
Natural variant | VAR_018719 | 183 | in HMND5; does not complement the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly interacts with NRP1; dbSNP:rs137852644 | |||
Sequence: L → P | ||||||
Natural variant | VAR_073188 | 200 | in CMT2D and HMND5; shows a large reduction in aminoacylation activity; dbSNP:rs1554337369 | |||
Sequence: D → N | ||||||
Natural variant | VAR_074016 | 200 | in CMT2D; dbSNP:rs1554337369 | |||
Sequence: D → Y | ||||||
Mutagenesis | 211 | Displays 62% of wild-type catalytic activity. Displays 20% of wild-type catalytic activity; when associated with G-125. | ||||
Sequence: C → R | ||||||
Natural variant | VAR_073189 | 265 | in CMT2D and HMND5; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules; dbSNP:rs1554337974 | |||
Sequence: S → F | ||||||
Natural variant | VAR_085141 | 265 | in CMT2D; uncertain significance; dbSNP:rs1554337974 | |||
Sequence: S → Y | ||||||
Natural variant | VAR_054866 | 268 | found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; uncertain significance; dbSNP:rs2230310 | |||
Sequence: T → I | ||||||
Natural variant | VAR_074017 | 292 | in CMT2D; dbSNP:rs1064795123 | |||
Sequence: M → R | ||||||
Natural variant | VAR_018720 | 294 | in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability; contrary to the wild-type protein, strongly interacts with NRP1; dbSNP:rs137852643 | |||
Sequence: G → R | ||||||
Natural variant | VAR_073190 | 298 | in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; dbSNP:rs137852648 | |||
Sequence: P → L | ||||||
Natural variant | VAR_079827 | 310 | found in a patient with growth retardation, microcephaly, thinning of the corpus callosum, decreased white matter and brain stem involvement, as well as large calvaria, cerebellar vermis atrophy, dysmorphic features, prominent epicanthal folds, hypotelorism, high-arched palate, delayed motor milestones, apnea and sparse thin scalp hair; likely pathogenic; reduces to less than 1% aminoacylation activity; dbSNP:rs1135401748 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_073191 | 334 | in CMT2D; uncertain significance; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; dbSNP:rs1554338260 | |||
Sequence: I → F | ||||||
Natural variant | VAR_085142 | 334 | in SMAJI; loss of function; based on yeast complementation assay; dbSNP:rs1554338262 | |||
Sequence: I → N | ||||||
Mutagenesis | 337 | Decrease in catalytic activity by more than 10-fold. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_054867 | 388 | in dbSNP:rs17159287 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_079828 | 412 | found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; uncertain significance; dbSNP:rs770924455 | |||
Sequence: R → C | ||||||
Natural variant | VAR_073192 | 472 | in HMND5; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast; dbSNP:rs1060502838 | |||
Sequence: H → R | ||||||
Mutagenesis | 486-490 | Loss of catalytic activity. | ||||
Sequence: Missing | ||||||
Natural variant | VAR_073193 | 554 | in CMT2D; demonstrates no change in subcellular location pattern; dbSNP:rs137852647 | |||
Sequence: D → N | ||||||
Natural variant | VAR_018721 | 580 | in HMND5; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity; dbSNP:rs137852646 | |||
Sequence: G → R | ||||||
Natural variant | VAR_079829 | 598 | in HMND5; uncertain significance; dbSNP:rs766280100 | |||
Sequence: G → A | ||||||
Mutagenesis | 602 | Decrease in catalytic activity by more than 10-fold. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_073194 | 635 | has no effect on subcellular localization; results in decreased affinity for glycine; dbSNP:rs201358272 | |||
Sequence: S → L | ||||||
Natural variant | VAR_073195 | 652 | in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; dbSNP:rs747080824 | |||
Sequence: G → A | ||||||
Natural variant | VAR_085143 | 652 | in SMAJI; dbSNP:rs1783251037 | |||
Sequence: G → R | ||||||
Mutagenesis | 658 | Decrease in catalytic activity by more than 10-fold. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 729 | Decrease in catalytic activity by about 10-fold. | ||||
Sequence: Q → A or N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 841 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, modified residue, modified residue (large scale data), chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-36 | UniProt | Mitochondrion | ||||
Sequence: MPSPRPVLLRGARAALLLLLPPRLLARPSLLLRRSL | |||||||
Modified residue | 35 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000072998 | 37-739 | UniProt | Glycine--tRNA ligase | |||
Sequence: SAASCPPISLPAAASRSSMDGAGAEEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKTPHTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVEARYPLFEGQETGKKETIEE | |||||||
Modified residue | 204 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 335 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 453 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 467 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 501 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 700 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 736 | UniProt | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P41250 | BATF Q16520 | 3 | EBI-724143, EBI-749503 | |
BINARY | P41250 | COPS3 Q9UNS2 | 3 | EBI-724143, EBI-350590 | |
BINARY | P41250 | GARS1 P41250 | 4 | EBI-724143, EBI-724143 | |
XENO | P41250 | Gars1 Q9CZD3 | 2 | EBI-724143, EBI-8321941 | |
BINARY | P41250 | KLF6 Q99612 | 3 | EBI-724143, EBI-714994 | |
BINARY | P41250 | PCDHGC3 Q9BR81 | 3 | EBI-724143, EBI-22012354 | |
BINARY | P41250 | SOCS4 Q8WXH5 | 3 | EBI-724143, EBI-3942425 | |
BINARY | P41250 | SPAG8 Q99932-2 | 3 | EBI-724143, EBI-11959123 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 63-119 | WHEP-TRS | ||||
Sequence: VLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIV |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative initiation.
P41250-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length739
- Mass (Da)83,166
- Last updated2010-11-30 v3
- ChecksumE4C001CEBF985C59
P41250-2
- Name2
- NoteThe isoform 2 translation is regulated by an Internal Ribosome Entry Site (IRES) and an upstream Open Reading Frame. Both are important in hindering the synthesis of the mitochondrial GARS and target the translation of the cytosolic enzyme to ER-bound ribosomes.
- Differences from canonical
- 1-54: Missing
Computationally mapped potential isoform sequences
There are 17 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6Q8PFV5 | A0A6Q8PFV5_HUMAN | GARS1 | 190 | ||
A0A6Q8PFZ6 | A0A6Q8PFZ6_HUMAN | GARS1 | 546 | ||
A0A6Q8PFN0 | A0A6Q8PFN0_HUMAN | GARS1 | 79 | ||
A0A6Q8PFU7 | A0A6Q8PFU7_HUMAN | GARS1 | 165 | ||
A0A6Q8PGI6 | A0A6Q8PGI6_HUMAN | GARS1 | 672 | ||
A0A6Q8PGN7 | A0A6Q8PGN7_HUMAN | GARS1 | 260 | ||
A0A6Q8PGA8 | A0A6Q8PGA8_HUMAN | GARS1 | 683 | ||
A0A6Q8PGT3 | A0A6Q8PGT3_HUMAN | GARS1 | 135 | ||
A0A6Q8PGZ8 | A0A6Q8PGZ8_HUMAN | GARS1 | 745 | ||
A0A6Q8PGZ9 | A0A6Q8PGZ9_HUMAN | GARS1 | 245 | ||
A0A6Q8PGW4 | A0A6Q8PGW4_HUMAN | GARS1 | 616 | ||
A0A6Q8PH49 | A0A6Q8PH49_HUMAN | GARS1 | 350 | ||
A0A6Q8PF45 | A0A6Q8PF45_HUMAN | GARS1 | 350 | ||
A0A6Q8PHH9 | A0A6Q8PHH9_HUMAN | GARS1 | 705 | ||
A0A6Q8PHI7 | A0A6Q8PHI7_HUMAN | GARS1 | 606 | ||
F8WCK4 | F8WCK4_HUMAN | GARS1 | 255 | ||
H7C443 | H7C443_HUMAN | GARS1 | 570 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_060970 | 1-54 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 9-18 | in Ref. 3; BAG58412 | ||||
Sequence: Missing | ||||||
Sequence conflict | 205 | in Ref. 3; BAG51964 | ||||
Sequence: D → G | ||||||
Sequence conflict | 530 | in Ref. 2; AAA86443 | ||||
Sequence: M → I | ||||||
Sequence conflict | 634 | in Ref. 3; BAG51964 | ||||
Sequence: L → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D30658 EMBL· GenBank· DDBJ | BAA06338.1 EMBL· GenBank· DDBJ | mRNA | ||
U09510 EMBL· GenBank· DDBJ | AAA86443.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK074524 EMBL· GenBank· DDBJ | BAG51964.1 EMBL· GenBank· DDBJ | mRNA | ||
AK295490 EMBL· GenBank· DDBJ | BAG58412.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005154 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC006969 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004976 EMBL· GenBank· DDBJ | AAC71652.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AACC02000087 EMBL· GenBank· DDBJ | EAL24449.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007722 EMBL· GenBank· DDBJ | AAH07722.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007755 EMBL· GenBank· DDBJ | AAH07755.1 EMBL· GenBank· DDBJ | mRNA | ||
U09587 EMBL· GenBank· DDBJ | AAA57001.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |