Q9Y4P1 · ATG4B_HUMAN
- ProteinCysteine protease ATG4B
- GeneATG4B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids393 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004, PubMed:26378241, PubMed:27527864, PubMed:28633005, PubMed:28821708, PubMed:29232556, PubMed:30076329, PubMed:30443548, PubMed:30661429).
Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed:33773106, PubMed:33909989).
The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:20818167, PubMed:21177865, PubMed:22302004, PubMed:27527864, PubMed:28287329, PubMed:28633005, PubMed:29458288, PubMed:30661429).
Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004).
Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106).
In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:15187094, PubMed:19322194, PubMed:28633005, PubMed:29458288, PubMed:32686895, PubMed:33909989).
Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:15187094, PubMed:19322194, PubMed:29458288, PubMed:32686895, PubMed:33909989).
Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989).
Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed:29458288, PubMed:30661429).
Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106).
Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed:33773106, PubMed:33909989).
The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:20818167, PubMed:21177865, PubMed:22302004, PubMed:27527864, PubMed:28287329, PubMed:28633005, PubMed:29458288, PubMed:30661429).
Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004).
Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106).
In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:15187094, PubMed:19322194, PubMed:28633005, PubMed:29458288, PubMed:32686895, PubMed:33909989).
Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:15187094, PubMed:19322194, PubMed:29458288, PubMed:32686895, PubMed:33909989).
Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989).
Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed:29458288, PubMed:30661429).
Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106).
Catalytic activity
- [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamineThis reaction proceeds in the forward direction.
- [protein]-C-terminal L-amino acid-glycyl-phosphatidylserine + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phospho-L-serineThis reaction proceeds in the forward direction.
Activity regulation
Inhibited by N-ethylmaleimide (PubMed:21177865).
Redox-regulated during autophagy since reducing conditions activate ATG4A whereas an oxidizing environment such as the presence of H2O2 inhibits its activity (PubMed:17347651).
The cysteine protease activity compounds is inhibited by styrylquinoline compounds 4-28 and LV-320 (PubMed:30076329).
Redox-regulated during autophagy since reducing conditions activate ATG4A whereas an oxidizing environment such as the presence of H2O2 inhibits its activity (PubMed:17347651).
The cysteine protease activity compounds is inhibited by styrylquinoline compounds 4-28 and LV-320 (PubMed:30076329).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
5.1 μM | MAP1LC3B | |||||
5.8 μM | GABARAP | |||||
4.4 μM | GABARAPL1 | |||||
6.1 μM | GABARAPL2 |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 74 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 278 | |||||
Sequence: D | ||||||
Active site | 280 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | autophagosome membrane | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | mitochondrion | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | cysteine-type peptidase activity | |
Molecular Function | endopeptidase activity | |
Molecular Function | protein-phosphatidylethanolamide deconjugating activity | |
Molecular Function | scaffold protein binding | |
Biological Process | aggrephagy | |
Biological Process | autophagosome assembly | |
Biological Process | autophagy | |
Biological Process | macroautophagy | |
Biological Process | microautophagy | |
Biological Process | mitophagy | |
Biological Process | otolith mineralization completed early in development | |
Biological Process | piecemeal microautophagy of the nucleus | |
Biological Process | protein delipidation | |
Biological Process | protein localization to phagophore assembly site | |
Biological Process | protein processing | |
Biological Process | protein transport | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCysteine protease ATG4B
- 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 accessionQ9Y4P1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Decreased phosphorylation by AKT2, leading to reduced proteolytic activation of ATG8 family proteins. | ||||
Sequence: S → A | ||||||
Mutagenesis | 34 | Phospho-mimetic mutant; increased proteolytic activation of ATG8 family proteins. | ||||
Sequence: S → D | ||||||
Mutagenesis | 74 | Complete loss of protease activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 78 | Reduces the redox sensitivity and retains activity in presence of H2O2. | ||||
Sequence: C → A | ||||||
Mutagenesis | 78 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 89 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 121 | Decreased phosphorylation by AKT2; when associated with A-262. | ||||
Sequence: S → A | ||||||
Mutagenesis | 142 | Strongly reduced protease activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 183 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 189 | Does not affect S-nitrosylation. Strongly decreased S-nitrosylation, leading to increased hydrolase activity and autophagic flux; when associated with S-292. Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 203 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 229 | Strongly reduced protease activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 246 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 262 | Decreased phosphorylation by AKT2; when associated with A-121. | ||||
Sequence: S → A | ||||||
Mutagenesis | 278 | Complete loss of protease activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 280 | Complete loss of protease activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 292 | Does not affect S-nitrosylation. Strongly decreased S-nitrosylation, leading to increased hydrolase activity and autophagic flux; when associated with S-189. Reduced formation of intrachain and interchain disulfide bonds in response to oxidation. Abolished formation of disulfide bonds, leading to increased autophagy; when associated with S-361. | ||||
Sequence: C → S | ||||||
Mutagenesis | 301 | Does not affect S-nitrosylation. Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 306 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 316 | Abolished phosphorylation by ULK1; promotes hydrolase activity, leading to increased proteolytic activation and delipidation of ATG8 family proteins. | ||||
Sequence: S → A | ||||||
Mutagenesis | 316 | Phospho-mimetic mutant; reduced hydrolase activity, leading to decreased proteolytic activation and delipidation of ATG8 family proteins. | ||||
Sequence: S → D | ||||||
Mutagenesis | 323 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Mutagenesis | 333 | Does not affect formation of disulfide bonds. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_021486 | 354 | in dbSNP:rs7601000 | |||
Sequence: L → Q | ||||||
Mutagenesis | 361 | Reduced formation of intrachain and interchain disulfide bonds in response to oxidation. Abolished formation of disulfide bonds, leading to increased autophagy; when associated with S-292. | ||||
Sequence: C → S | ||||||
Mutagenesis | 383 | Decreased phosphorylation, leading to decreased hydrolase activity and autophagic flux. Does not affect interaction with ATG8 family proteins. | ||||
Sequence: S → A | ||||||
Mutagenesis | 383 | Phospho-mimetic mutant; does not affect interaction with ATG8 family proteins. | ||||
Sequence: S → E | ||||||
Mutagenesis | 388-391 | In 2mLIR; decreased interaction with ATG8 family proteins MAP1LC3A, MAP1LC3B and MAP1LC3C. Decreased ability to mediate delipidation of ATG8 proteins conjugated to phosphatidylethanolamine (PE). | ||||
Sequence: FEIL → AEIA | ||||||
Mutagenesis | 392 | Decreased phosphorylation, leading to decreased hydrolase activity and autophagic flux. Does not affect interaction with ATG8 family proteins. | ||||
Sequence: S → A | ||||||
Mutagenesis | 392 | Phospho-mimetic mutant; slightly increased interaction with ATG8 family proteins. | ||||
Sequence: S → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 412 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000215844 | 1-393 | UniProt | Cysteine protease ATG4B | |||
Sequence: MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFIDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIPDESFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVELQPSHLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 34 | UniProt | Phosphoserine; by PKB/AKT1 and PKB/AKT2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 189 | UniProt | S-nitrosocysteine | ||||
Sequence: C | |||||||
Modified residue | 292 | UniProt | S-nitrosocysteine | ||||
Sequence: C | |||||||
Disulfide bond | 292 | UniProt | Interchain (with C-361) | ||||
Sequence: C | |||||||
Disulfide bond | 292↔361 | UniProt | |||||
Sequence: CFIPDESFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVELQPSHLAC | |||||||
Modified residue | 301 | UniProt | S-nitrosocysteine | ||||
Sequence: C | |||||||
Modified residue | 316 | UniProt | Phosphoserine; by ULK1 | ||||
Sequence: S | |||||||
Disulfide bond | 361 | UniProt | Interchain (with C-292) | ||||
Sequence: C | |||||||
Modified residue | 383 | UniProt | Phosphoserine; by STK26 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 392 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-383 and Ser-392 promotes autophagy by increasing protein delipidation activity without affecting proteolytic activation of ATG8 proteins (PubMed:26378241).
Phosphorylation at Ser-316 by ULK1 inhibits autophagy by decreasing both proteolytic activation and delipidation activities (PubMed:28821708).
Phosphorylation at Ser-316 is dephosphorylated by protein phosphatase 2A (PP2A) (PubMed:28821708).
Phosphorylation at Ser-34 by AKT2 promotes its hydrolase activity, leading to increased proteolytic activation and delipidation of ATG8 family proteins (PubMed:30443548).
Phosphorylation at Ser-34 by AKT1 promotes mitochondrial localization and inhibition of the F1F0-ATP synthase activity, leading to elevation of mitochondrial reactive oxygen species (ROS) (PubMed:29165041).
Phosphorylation at Ser-316 by ULK1 inhibits autophagy by decreasing both proteolytic activation and delipidation activities (PubMed:28821708).
Phosphorylation at Ser-316 is dephosphorylated by protein phosphatase 2A (PP2A) (PubMed:28821708).
Phosphorylation at Ser-34 by AKT2 promotes its hydrolase activity, leading to increased proteolytic activation and delipidation of ATG8 family proteins (PubMed:30443548).
Phosphorylation at Ser-34 by AKT1 promotes mitochondrial localization and inhibition of the F1F0-ATP synthase activity, leading to elevation of mitochondrial reactive oxygen species (ROS) (PubMed:29165041).
Ubiquitinated by RNF5, leading to its degradation by the proteasome.
S-nitrosylation at Cys-189 and Cys-292 in response to high glucose decreases both proteolytic activation and delipidation activities.
O-glycosylated by OGT, leading to increase protease activity, thereby promoting the proteolytic activation of ATG8 family proteins.
Forms reversible intrachain disulfide bonds in response to oxidative stress (PubMed:31880198).
Forms interchain disulfide bonds, leading to formation of homooligomers in response to oxidation (PubMed:31880198).
Forms interchain disulfide bonds, leading to formation of homooligomers in response to oxidation (PubMed:31880198).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with PFKP; promoting phosphorylation of ATG4B at Ser-34 (PubMed:33607258).
Interacts with GBP7 (By similarity).
Interacts with GBP7 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9Y4P1 | ERDMAN_2289 A0A0H3LAC5 | 2 | EBI-712014, EBI-25401874 | |
BINARY | Q9Y4P1 | GABARAP O95166 | 9 | EBI-712014, EBI-712001 | |
BINARY | Q9Y4P1 | GABARAPL1 Q9H0R8 | 12 | EBI-712014, EBI-746969 | |
BINARY | Q9Y4P1 | GABARAPL2 P60520 | 12 | EBI-712014, EBI-720116 | |
BINARY | Q9Y4P1 | MAP1LC3A Q9H492 | 6 | EBI-712014, EBI-720768 | |
BINARY | Q9Y4P1 | MAP1LC3B Q9GZQ8 | 15 | EBI-712014, EBI-373144 | |
BINARY | Q9Y4P1 | MAP1LC3C Q9BXW4 | 4 | EBI-712014, EBI-2603996 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 388-391 | LIR | ||||
Sequence: FEIL |
Domain
The LIR motif (LC3-interacting region) is required for the interaction with ATG8 family proteins MAP1LC3A, MAP1LC3B, MAP1LC3C and GABARAPL1 (PubMed:28287329).
Required for proteolytic activation and delipidation of ATG8 proteins (PubMed:28287329, PubMed:29458288).
Required for proteolytic activation and delipidation of ATG8 proteins (PubMed:28287329, PubMed:29458288).
Sequence similarities
Belongs to the peptidase C54 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q9Y4P1-1
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
- Length393
- Mass (Da)44,294
- Last updated2010-05-18 v2
- ChecksumF4ADB3192176E0E5
Q9Y4P1-2
- Name2
Q9Y4P1-3
- Name3
Q9Y4P1-4
- Name4
Q9Y4P1-6
- Name6
- Differences from canonical
- 370-393: DSSDVERLERFFDSEDEDFEILSL → GESCQVQILLM
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_013029 | 1 | in isoform 2 | |||
Sequence: M → MAHSVPSDSRTSRRPTTRPHAARGAPRGSRRPGRTPKWRLPRISARAPYRLRRLRRHTYWPPRRPVAASRCWPVGATPLGSVGGRTGKM | ||||||
Alternative sequence | VSP_013028 | 1-74 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 136 | in Ref. 3; BAB83890 | ||||
Sequence: Missing | ||||||
Sequence conflict | 188 | in Ref. 6; BAB55127 | ||||
Sequence: P → L | ||||||
Sequence conflict | 247 | in Ref. 6; BAB55353 | ||||
Sequence: F → Y | ||||||
Sequence conflict | 273 | in Ref. 6; BAB55042 | ||||
Sequence: E → G | ||||||
Sequence conflict | 312 | in Ref. 3; BAB83890 | ||||
Sequence: E → N | ||||||
Alternative sequence | VSP_013031 | 321-354 | in isoform 3 | |||
Sequence: FFCKTEDDFNDWCQQVKKLSLLGGALPMFELVEL → KQGRLVRSLIPWAPRPSSWCAAVLGAAVVMCGTP | ||||||
Alternative sequence | VSP_013032 | 355-393 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013033 | 369 | in isoform 4 | |||
Sequence: L → LGESCQVQVGSLG | ||||||
Alternative sequence | VSP_013034 | 370-393 | in isoform 2 and isoform 6 | |||
Sequence: DSSDVERLERFFDSEDEDFEILSL → GESCQVQILLM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ504652 EMBL· GenBank· DDBJ | CAD43219.1 EMBL· GenBank· DDBJ | mRNA | ||
AB066215 EMBL· GenBank· DDBJ | BAB83890.1 EMBL· GenBank· DDBJ | mRNA | ||
AB023160 EMBL· GenBank· DDBJ | BAA76787.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK027332 EMBL· GenBank· DDBJ | BAB55042.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027462 EMBL· GenBank· DDBJ | BAB55127.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027763 EMBL· GenBank· DDBJ | BAB55353.1 EMBL· GenBank· DDBJ | mRNA | ||
AK125277 EMBL· GenBank· DDBJ | BAC86110.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL080168 EMBL· GenBank· DDBJ | CAB45756.1 EMBL· GenBank· DDBJ | mRNA | ||
AC133528 EMBL· GenBank· DDBJ | AAY14919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000719 EMBL· GenBank· DDBJ | AAH00719.1 EMBL· GenBank· DDBJ | mRNA |