O60343 · TBCD4_HUMAN
- ProteinTBC1 domain family member 4
- GeneTBC1D4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1298 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | vesicle | |
Molecular Function | GTPase activator activity | |
Biological Process | cellular response to insulin stimulus | |
Biological Process | negative regulation of vesicle fusion | |
Biological Process | vesicle-mediated transport |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTBC1 domain family member 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60343
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Type 2 diabetes mellitus 5 (T2D5)
- Note
- DescriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
- See alsoMIM:616087
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 318 | 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-588; A-642 and A-751. | ||||
Sequence: S → A | ||||||
Mutagenesis | 588 | 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-642 and A-751. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_061891 | 619 | in dbSNP:rs56223054 | |||
Sequence: P → L | ||||||
Mutagenesis | 642 | 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-751. | ||||
Sequence: T → A | ||||||
Mutagenesis | 751 | 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-642. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_059855 | 819 | in dbSNP:rs1062087 | |||
Sequence: V → I | ||||||
Mutagenesis | 972 | Loss of Rab GTPase activation. Only 20% reduction of GLUT4 translocation; even when associated with A-318; A-588; A-642 and A-751. | ||||
Sequence: R → K | ||||||
Natural variant | VAR_061892 | 1119 | in dbSNP:rs58232698 | |||
Sequence: V → A | ||||||
Natural variant | VAR_052534 | 1147 | in dbSNP:rs9600455 | |||
Sequence: T → M | ||||||
Natural variant | VAR_052535 | 1275 | in dbSNP:rs557337 | |||
Sequence: V → A | ||||||
Natural variant | VAR_054862 | 1284 | in dbSNP:rs11616741 | |||
Sequence: L → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,492 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000208026 | 1-1298 | UniProt | TBC1 domain family member 4 | |||
Sequence: MEPPSCIQDEPFPHPLEPEPGVSAQPGPGKPSDKRFRLWYVGGSCLDHRTTLPMLPWLMAEIRRRSQKPEAGGCGAPAAREVILVLSAPFLRCVPAPGAGASGGTSPSATQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPSQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGKVTVTHKKAPSSLIDDCMEKFSLHEQQRLKIQGEQRGPDPGEDLADLEVVVPGSPGDCLPEEADGTDTHLGLPAGASQPALTSSRVCFPERILEDSGFDEQQEFRSRCSSVTGVQRRVHEGSQKSQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLTLKQAFSTAAALQSAKTQIKLCEACPMHSLHKLCERIEGLYPPRAKLVIQRHLSSLTDNEQADIFERVQKMKPVSDQEENELVILHLRQLCEAKQKTHVHIGEGPSTISNSTIPENATSSGRFKLDILKNKAKRSLTSSLENIFSRGANRMRGRLGSVDSFERSNSLASEKDYSPGDSPPGTPPASPPSSAWQTFPEEDSDSPQFRRRAHTFSHPPSSTKRKLNLQDGRAQGVRSPLLRQSSSEQCSNLSSVRRMYKESNSSSSLPSLHTSFSAPSFTAPSFLKSFYQNSGRLSPQYENEIRQDTASESSDGEGRKRTSSTCSNESLSVGGTSVTPRRISWRQRIFLRVASPMNKSPSAMQQQDGLDRNELLPLSPLSPTMEEEPLVVFLSGEDDPEKIEERKKSKELRSLWRKAIHQQILLLRMEKENQKLEASRDELQSRKVKLDYEEVGACQKEVLITWDKKLLNCRAKIRCDMEDIHTLLKEGVPKSRRGEIWQFLALQYRLRHRLPNKQQPPDISYKELLKQLTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQGTEVIFKVALSLLSSQETLIMECESFENIVEFLKNTLPDMNTSEMEKIITQVFEMDISKQLHAYEVEYHVLQDELQESSYSCEDSETLEKLERANSQLKRQNMDLLEKLQVAHTKIQALESNLENLLTRETKMKSLIRTLEQEKMAYQKTVEQLRKLLPADALVNCDLLLRDLNCNPNNKAKIGNKP | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 262 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 314 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 318 | UniProt | Phosphoserine; by PKB/AKT1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 341 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 344 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 477 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 485 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 566 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 566 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 568 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 570 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 570 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 577 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 588 | UniProt | Phosphoserine; by PKB/AKT1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 591 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 591 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 597 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 609 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 609 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 613 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 617 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 617 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 642 | UniProt | Phosphothreonine; by PKB/AKT1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 644 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 648 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 650 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 666 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 666 | UniProt | In isoform O60343-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 666 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 672 | UniProt | In isoform O60343-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 673 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 678 | UniProt | In isoform O60343-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 698 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 749 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 750 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 751 | UniProt | Phosphoserine; by PKB/AKT1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 751 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 752 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 754 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 754 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 757 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 763 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 782 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 787 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 789 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1207 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by AKT1; insulin-induced. Also phosphorylated by AMPK in response to insulin. Insulin-stimulated phosphorylation is required for SLC2A4/GLUT4 translocation. Has no effect on SLC2A4/GLUT4 internalization. Physiological hyperinsulinemia increases phosphorylation in skeletal muscle. Insulin-stimulated phosphorylation is reduced by 39% in type 2 diabetic patients.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Isoform 2 is the highest overexpressed in most tissues. Isoform 1 is highly expressed in skeletal muscle and heart, but was not detectable in the liver nor in adipose tissue. Isoform 2 is strongly expressed in adrenal and thyroid gland, and also in lung, kidney, colon, brain and adipose tissue. Isoform 2 is moderately expressed in skeletal muscle. Expressed in pancreatic Langerhans islets, including beta cells (at protein level). Expression is decreased by twofold in pancreatic islets in type 2 diabetes patients compared to control subjects. Up-regulated in T-cells from patients with atopic dermatitis.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O60343 | SFN P31947 | 4 | EBI-522028, EBI-476295 | |
BINARY | O60343 | YWHAE P62258 | 6 | EBI-522028, EBI-356498 | |
BINARY | O60343 | YWHAZ P63104 | 5 | EBI-522028, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-25 | Pro residues | ||||
Sequence: MEPPSCIQDEPFPHPLEPEPGVSAQ | ||||||
Region | 1-31 | Disordered | ||||
Sequence: MEPPSCIQDEPFPHPLEPEPGVSAQPGPGKP | ||||||
Domain | 53-209 | PID 1 | ||||
Sequence: PMLPWLMAEIRRRSQKPEAGGCGAPAAREVILVLSAPFLRCVPAPGAGASGGTSPSATQPNPAVFIFEHKAQHISRFIHNSHDLTYFAYLIKAQPDDPESQMACHVFRATDPSQVPDVISSIRQLSKAAMKEDAKPSKDNEDAFYNSQKFEVLYCGK | ||||||
Region | 241-287 | Disordered | ||||
Sequence: GEQRGPDPGEDLADLEVVVPGSPGDCLPEEADGTDTHLGLPAGASQP | ||||||
Domain | 312-468 | PID 2 | ||||
Sequence: FRSRCSSVTGVQRRVHEGSQKSQPRRRHASAPSHVQPSDSEKNRTMLFQVGRFEINLISPDTKSVVLEKNFKDISSCSQGIKHVDHFGFICRESPEPGLSQYICYVFQCASESLVDEVMLTLKQAFSTAAALQSAKTQIKLCEACPMHSLHKLCERI | ||||||
Region | 317-353 | Disordered | ||||
Sequence: SSVTGVQRRVHEGSQKSQPRRRHASAPSHVQPSDSEK | ||||||
Region | 586-685 | Disordered | ||||
Sequence: LGSVDSFERSNSLASEKDYSPGDSPPGTPPASPPSSAWQTFPEEDSDSPQFRRRAHTFSHPPSSTKRKLNLQDGRAQGVRSPLLRQSSSEQCSNLSSVRR | ||||||
Compositional bias | 666-685 | Polar residues | ||||
Sequence: SPLLRQSSSEQCSNLSSVRR | ||||||
Region | 725-765 | Disordered | ||||
Sequence: SPQYENEIRQDTASESSDGEGRKRTSSTCSNESLSVGGTSV | ||||||
Compositional bias | 747-765 | Polar residues | ||||
Sequence: KRTSSTCSNESLSVGGTSV | ||||||
Domain | 918-1112 | Rab-GAP TBC | ||||
Sequence: GVPKSRRGEIWQFLALQYRLRHRLPNKQQPPDISYKELLKQLTAQQHAILVDLGRTFPTHPYFSVQLGPGQLSLFNLLKAYSLLDKEVGYCQGISFVAGVLLLHMSEEQAFEMLKFLMYDLGFRKQYRPDMMSLQIQMYQLSRLLHDYHRDLYNHLEENEISPSLYAAPWFLTLFASQFSLGFVARVFDIIFLQG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
O60343-1
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
- Length1,298
- Mass (Da)146,563
- Last updated2005-06-07 v2
- Checksum8DC70CE887C0B311
O60343-2
- Name2
- SynonymsAS160_tv2
- Differences from canonical
- 678-740: Missing
O60343-3
- Name3
- SynonymsAS160_tv3
- Differences from canonical
- 733-740: Missing
O60343-4
- Name4
O60343-5
- Name5
- Differences from canonical
- 1-783: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5JU47 | Q5JU47_HUMAN | TBC1D4 | 282 | ||
A0A3B3IRT3 | A0A3B3IRT3_HUMAN | TBC1D4 | 1054 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-25 | Pro residues | ||||
Sequence: MEPPSCIQDEPFPHPLEPEPGVSAQ | ||||||
Alternative sequence | VSP_036868 | 1-783 | in isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 644 | in Ref. 7; CAH18416 | ||||
Sequence: S → G | ||||||
Compositional bias | 666-685 | Polar residues | ||||
Sequence: SPLLRQSSSEQCSNLSSVRR | ||||||
Alternative sequence | VSP_036869 | 678-740 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_036870 | 733-740 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 747-765 | Polar residues | ||||
Sequence: KRTSSTCSNESLSVGGTSV | ||||||
Sequence conflict | 845 | in Ref. 7; CAH18416 | ||||
Sequence: K → E | ||||||
Sequence conflict | 864 | in Ref. 2; BAH16628, 3; BAA25529 and 6; AAI51240 | ||||
Sequence: E → EG | ||||||
Alternative sequence | VSP_036871 | 865-917 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 867 | in Ref. 7; CAH18416 | ||||
Sequence: R → G | ||||||
Sequence conflict | 1137 | in Ref. 7; CAH18416 | ||||
Sequence: F → L | ||||||
Sequence conflict | 1178 | in Ref. 4; BAG62187 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FM207106 EMBL· GenBank· DDBJ | CAR62509.1 EMBL· GenBank· DDBJ | mRNA | ||
FM207107 EMBL· GenBank· DDBJ | CAR62510.1 EMBL· GenBank· DDBJ | mRNA | ||
AB449885 EMBL· GenBank· DDBJ | BAH16628.1 EMBL· GenBank· DDBJ | mRNA | ||
AB011175 EMBL· GenBank· DDBJ | BAA25529.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK300468 EMBL· GenBank· DDBJ | BAG62187.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304091 EMBL· GenBank· DDBJ | BAG64997.1 EMBL· GenBank· DDBJ | mRNA | ||
AL139230 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL162571 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC151239 EMBL· GenBank· DDBJ | AAI51240.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749622 EMBL· GenBank· DDBJ | CAH18416.1 EMBL· GenBank· DDBJ | mRNA |