O75030 · MITF_HUMAN
- ProteinMicrophthalmia-associated transcription factor
- GeneMITF
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids526 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoter of pigmentation genes, such as tyrosinase (TYR) (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758).
Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, MITF phosphorylation by MTOR promotes its inactivation (PubMed:36608670).
Upon starvation or lysosomal stress, inhibition of MTOR induces MITF dephosphorylation, resulting in transcription factor activity (PubMed:36608670).
Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1) (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758).
Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758).
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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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrophthalmia-associated transcription factor
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75030
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phosphorylation by MTOR promotes ubiquitination and degradation (PubMed:36608670).
Conversely, inhibition of mTORC1, starvation and lysosomal disruption, promotes dephosphorylation and translocation to the nucleus (PubMed:36608670).
Phosphorylation by MARK3/cTAK1 promotes association with 14-3-3/YWHA adapters and retention in the cytosol (PubMed:16822840).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Waardenburg syndrome 2A (WS2A)
- Note
- DescriptionWS2 is a genetically heterogeneous, autosomal dominant disorder characterized by sensorineural deafness, pigmentary disturbances, and absence of dystopia canthorum. The frequency of deafness is higher in WS2 than in WS1.
- See alsoMIM:193510
Natural variants in WS2A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078311 | 294 | A>T | in WS2A; uncertain significance; dbSNP:rs1559742541 | |
VAR_010297 | 310 | R>K | in WS2A; uncertain significance | |
VAR_010299 | 324 | missing | in WS2A and COMMAD; does not localize to the nucleus; does not bind M-box or E-box DNA sequences; loss of function in transcriptional regulation; dominant negative effect; dbSNP:rs1553704814 | |
VAR_010300 | 357 | S>P | in WS2A; dbSNP:rs104893744 | |
VAR_010301 | 385 | N>D | in WS2A | |
VAR_010302 | 405 | S>P | in WS2A; dbSNP:rs104893747 |
Tietz albinism-deafness syndrome (TADS)
- Note
- DescriptionAn autosomal dominant disorder characterized by generalized hypopigmentation and congenital, bilateral, profound sensorineural deafness.
- See alsoMIM:103500
Natural variants in TADS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_010298 | 317 | N>K | in TADS; dbSNP:rs104893745 |
Melanoma, cutaneous malignant 8 (CMM8)
- Note
- DescriptionA malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but may also involve other sites.
- See alsoMIM:614456
Coloboma, osteopetrosis, microphthalmia, macrocephaly, albinism, and deafness (COMMAD)
- Note
- DescriptionAn autosomal recessive syndrome characterized by severe microphthalmia, profound congenital sensorineural hearing loss, lack of pigment in the hair, skin, and eyes, macrocephaly, facial dysmorphism, and osteopetrosis.
- See alsoMIM:617306
Natural variants in COMMAD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_077922 | 313 | K>N | in COMMAD; has both cytoplasmic and nuclear localization; decreased binding to M-box or E-box DNA sequences; dbSNP:rs1057519325 | |
VAR_077923 | 324 | R>G | in COMMAD; dbSNP:rs1057519326 | |
VAR_010299 | 324 | missing | in WS2A and COMMAD; does not localize to the nucleus; does not bind M-box or E-box DNA sequences; loss of function in transcriptional regulation; dominant negative effect; dbSNP:rs1553704814 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 5 | Impaired phosphorylation by MTOR, leading to abolished ubiquitination and degradation by the SCF(BTRC) complex. | ||||
Sequence: S → A | ||||||
Mutagenesis | 180 | Abolishes both transcription factor activity and ubiquitination, leading to an inert and stable protein; when associated with A-516. | ||||
Sequence: S → A | ||||||
Mutagenesis | 280 | Accumulates in the nucleus due to impaired phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 289 | Loss of sumoylation; when associated with R-423. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_078311 | 294 | in WS2A; uncertain significance; dbSNP:rs1559742541 | |||
Sequence: A → T | ||||||
Natural variant | VAR_010297 | 310 | in WS2A; uncertain significance | |||
Sequence: R → K | ||||||
Natural variant | VAR_077922 | 313 | in COMMAD; has both cytoplasmic and nuclear localization; decreased binding to M-box or E-box DNA sequences; dbSNP:rs1057519325 | |||
Sequence: K → N | ||||||
Natural variant | VAR_010298 | 317 | in TADS; dbSNP:rs104893745 | |||
Sequence: N → K | ||||||
Natural variant | VAR_077923 | 324 | in COMMAD; dbSNP:rs1057519326 | |||
Sequence: R → G | ||||||
Natural variant | VAR_010299 | 324 | in WS2A and COMMAD; does not localize to the nucleus; does not bind M-box or E-box DNA sequences; loss of function in transcriptional regulation; dominant negative effect; dbSNP:rs1553704814 | |||
Sequence: Missing | ||||||
Natural variant | VAR_010300 | 357 | in WS2A; dbSNP:rs104893744 | |||
Sequence: S → P | ||||||
Natural variant | VAR_010301 | 385 | in WS2A | |||
Sequence: N → D | ||||||
Natural variant | VAR_010302 | 405 | in WS2A; dbSNP:rs104893747 | |||
Sequence: S → P | ||||||
Mutagenesis | 405 | Loss of phosphorylation and function. | ||||
Sequence: S → A or P | ||||||
Mutagenesis | 423 | Loss of sumoylation; when associated with R-289. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_067367 | 425 | risk factor for CMM8; risk factor for pheochromocytomas and paragangliomas; results in impaired sumoylation; dbSNP:rs149617956 | |||
Sequence: E → K | ||||||
Mutagenesis | 516 | Abolishes both transcription factor activity and ubiquitination, leading to an inert and stable protein; when associated with A-180. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,115 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 chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000127276 | 1-526 | UniProt | Microphthalmia-associated transcription factor | |||
Sequence: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRQQVKQYLSTTLANKHANQVLSLPCPNQPGDHVMPPVPGSSAPNSPMAMLTLNSNCEKEGFYKFEEQNRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYGNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKELENRQKKLEHANRHLLLRIQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQDLLQHHADLTCTTTLDLTDGTITFNNNLGTGTEANQAYSVPTKMGSKLEDILMDDTLSPVGVTDPLLSSVSPGASKTSSRRSSMSMEETEHTC | |||||||
Modified residue | 5 | UniProt | Phosphoserine; by MTOR | ||||
Sequence: S | |||||||
Modified residue | 180 | UniProt | Phosphoserine; by MAPK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 280 | UniProt | Phosphoserine; by MARK3 | ||||
Sequence: S | |||||||
Cross-link | 289 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue | 405 | UniProt | Phosphoserine; by GSK3 | ||||
Sequence: S | |||||||
Modified residue | 414 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 423 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 491 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 516 | UniProt | Phosphoserine; by RPS6KA1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-405 significantly enhances the ability to bind the tyrosinase promoter (PubMed:10587587).
Phosphorylation by MARK3/cTAK1 at Ser-280 promotes association with 14-3-3/YWHA adapters and retention in the cytosol (PubMed:16822840).
Phosphorylated at Ser-180 and Ser-516 following KIT signaling, triggering a short live activation: Phosphorylation at Ser-180 and Ser-516 by MAPK and RPS6KA1, respectively, activate the transcription factor activity but also promote ubiquitination and subsequent degradation by the proteasome (PubMed:10673502).
Phosphorylated in response to blue light (415nm) (PubMed:28842328).
Ubiquitinated following phosphorylation at Ser-180, leading to subsequent degradation by the proteasome (PubMed:10673502).
Deubiquitinated by USP13, preventing its degradation (PubMed:10673502).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform A2
Expressed in the kidney (PubMed:10578055, PubMed:9647758).
Isoform C2
Isoform H1
Isoform H2
Isoform M1
Isoform Mdel
Gene expression databases
Organism-specific databases
Interaction
Subunit
Efficient DNA binding requires dimerization with another bHLH protein (PubMed:14975237).
Binds DNA in the form of homodimer or heterodimer with either TFE3, TFEB or TFEC (PubMed:15507434).
Interacts with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD); promoting its recruitment to lysosomal membrane in the presence of nutrients (PubMed:23401004, PubMed:36608670).
Interacts with KARS1 (PubMed:14975237).
Identified in a complex with HINT1 and CTNNB1 (PubMed:22647378).
Interacts with VSX2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75030 | SUMO1 P63165 | 2 | EBI-3910192, EBI-80140 | |
BINARY | O75030 | TFE3 P19532 | 2 | EBI-3910192, EBI-1048957 | |
BINARY | O75030 | TFEB P19484 | 3 | EBI-3910192, EBI-2814208 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-54 | Disordered | ||||
Sequence: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMT | ||||||
Compositional bias | 11-26 | Basic and acidic residues | ||||
Sequence: FEVGEEFHEEPKTYYE | ||||||
Compositional bias | 28-54 | Polar residues | ||||
Sequence: KSQPLKSSSSAEHPGASKPPISSSSMT | ||||||
Region | 224-295 | Transactivation | ||||
Sequence: DDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYGNQGLPPPGLTISNSCPANLPNIKRELTAC | ||||||
Domain | 311-364 | bHLH | ||||
Sequence: QKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKL | ||||||
Coiled coil | 355-402 | |||||
Sequence: KASVDYIRKLQREQQRAKELENRQKKLEHANRHLLLRIQELEMQARAH | ||||||
Region | 374-395 | Leucine-zipper | ||||
Sequence: LENRQKKLEHANRHLLLRIQEL | ||||||
Region | 401-431 | DNA-binding regulation | ||||
Sequence: AHGLSLIPSTGLCSPDLVNRIIKQEPVLENC | ||||||
Compositional bias | 496-515 | Polar residues | ||||
Sequence: TDPLLSSVSPGASKTSSRRS | ||||||
Region | 496-526 | Disordered | ||||
Sequence: TDPLLSSVSPGASKTSSRRSSMSMEETEHTC |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 12 isoforms produced by Alternative splicing. The X2-type isoforms differ from the X1-type isoforms by the absence of a 6 residue insert.
O75030-1
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.
- NameA1
- Length526
- Mass (Da)58,795
- Last updated2001-02-21 v2
- Checksum136EBED3044C1986
O75030-2
- NameA2
- Differences from canonical
- 294-299: Missing
O75030-3
- NameB1
- Differences from canonical
- 1-34: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MLYAFWFSH
O75030-4
- NameB2
O75030-5
- NameC1
- Differences from canonical
- 1-34: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MGHLENTSVVFPRAIFSLCEKETRKLTLCLFSR
O75030-6
- NameC2
O75030-7
- NameH1
- Differences from canonical
- 1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRVQMFMPCSFESLYL
O75030-8
- NameH2
O75030-9
- NameM1
- Differences from canonical
- 1-118: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLK → MLEMLEYNHYQ
O75030-10
- NameM2
O75030-11
- NameMdel
O75030-12
- Name12
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J845 | C9J845_HUMAN | MITF | 157 | ||
C9K0S7 | C9K0S7_HUMAN | MITF | 70 | ||
C9JBI8 | C9JBI8_HUMAN | MITF | 361 | ||
E9PKJ8 | E9PKJ8_HUMAN | MITF | 105 | ||
A0A8I5KRZ6 | A0A8I5KRZ6_HUMAN | MITF | 373 | ||
A0A8I5KTU3 | A0A8I5KTU3_HUMAN | MITF | 495 | ||
A0A8I5KSZ4 | A0A8I5KSZ4_HUMAN | MITF | 503 | ||
A0A087WXU1 | A0A087WXU1_HUMAN | MITF | 91 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002124 | 1-34 | in isoform B1 and isoform B2 | |||
Sequence: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MLYAFWFSH | ||||||
Alternative sequence | VSP_002125 | 1-34 | in isoform C1 and isoform C2 | |||
Sequence: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MGHLENTSVVFPRAIFSLCEKETRKLTLCLFSR | ||||||
Alternative sequence | VSP_002126 | 1-35 | in isoform H1 and isoform H2 | |||
Sequence: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRVQMFMPCSFESLYL | ||||||
Alternative sequence | VSP_046438 | 1-52 | in isoform 12 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002127 | 1-118 | in isoform M1, isoform M2 and isoform Mdel | |||
Sequence: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLK → MLEMLEYNHYQ | ||||||
Compositional bias | 11-26 | Basic and acidic residues | ||||
Sequence: FEVGEEFHEEPKTYYE | ||||||
Compositional bias | 28-54 | Polar residues | ||||
Sequence: KSQPLKSSSSAEHPGASKPPISSSSMT | ||||||
Alternative sequence | VSP_045178 | 139-194 | in isoform Mdel | |||
Sequence: Missing | ||||||
Sequence conflict | 241 | in Ref. 5; BAG58874 | ||||
Sequence: I → T | ||||||
Alternative sequence | VSP_045179 | 293-298 | in isoform Mdel and isoform 12 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002128 | 294-299 | in isoform A2, isoform B2, isoform C2, isoform H2 and isoform M2 | |||
Sequence: Missing | ||||||
Compositional bias | 496-515 | Polar residues | ||||
Sequence: TDPLLSSVSPGASKTSSRRS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB006909 EMBL· GenBank· DDBJ | BAA32288.1 EMBL· GenBank· DDBJ | mRNA | ||
AB006989 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
Z29678 EMBL· GenBank· DDBJ | CAA82775.1 EMBL· GenBank· DDBJ | mRNA | ||
GU355676 EMBL· GenBank· DDBJ | ADB90411.1 EMBL· GenBank· DDBJ | mRNA | ||
AL110195 EMBL· GenBank· DDBJ | CAB53672.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296129 EMBL· GenBank· DDBJ | BAG58874.1 EMBL· GenBank· DDBJ | mRNA | ||
AC099326 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104445 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104449 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC124915 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC026961 EMBL· GenBank· DDBJ | AAH26961.1 EMBL· GenBank· DDBJ | mRNA | ||
BC065243 EMBL· GenBank· DDBJ | AAH65243.1 EMBL· GenBank· DDBJ | mRNA | ||
AF034755 EMBL· GenBank· DDBJ | AAC39639.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB032359 EMBL· GenBank· DDBJ | BAA95208.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB032358 EMBL· GenBank· DDBJ | BAA95207.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB032357 EMBL· GenBank· DDBJ | BAA95206.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB009608 EMBL· GenBank· DDBJ | BAA95209.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. |