P49959 · MRE11_HUMAN
- ProteinDouble-strand break repair protein MRE11
- GeneMRE11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids708 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:24316220, PubMed:28867292, PubMed:31353207, PubMed:38128537).
The complex 1 mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is 2 required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:24316220, PubMed:27889449, PubMed:28867292, PubMed:36050397, PubMed:38128537).
Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:11741547, PubMed:22078559, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:29670289, PubMed:31353207, PubMed:36563124, PubMed:9590181, PubMed:9651580, PubMed:9705271).
After DSBs, MRE11 is loaded onto DSBs sites and cleaves DNA by cooperating with RBBP8/CtIP to initiate end resection (PubMed:27814491, PubMed:27889449, PubMed:30787182).
MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:24316220).
It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation to create entry sites for EXO1- and DNA2-mediated 5' to 3' long-range resection, which is required for single-strand invasion and recombination (PubMed:24316220, PubMed:28867292).
RBBP8/CtIP specifically promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182).
The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:14657032, PubMed:15064416, PubMed:15790808, PubMed:16622404).
The MRN complex is also required for the processing of R-loops (PubMed:31537797).
The MRN complex is involved in the activation of the cGAS-STING pathway induced by DNA damage during tumorigenesis: the MRN complex acts by displacing CGAS from nucleosome sequestration, thereby activating it (By similarity).
In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888).
Cofactor
Activity regulation
RBBP8/CtIP specifically promotes the endonuclease activity to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182).
DYNLL1-binding inhibits the activity of MRE11 (PubMed:30464262, PubMed:37696958).
MRE11 activity is inhibited by C1QBP: in absence of DNA damage, C1QBP interacts with unphosphorylated MRE11, preventing formation and activity of the MRN complex (PubMed:31353207).
The mirin-derivative PFM39, specifically inhibits the 3'-5' exonuclease activity (PubMed:24316220).
The N-alkylated mirin-derivatives PFM03 and PFM01 specifically inhibit the endonuclease activity (PubMed:24316220).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 20 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 22 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 60 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 60 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 128 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 129 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 217 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 245 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 247 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDouble-strand break repair protein MRE11
- 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 accessionP49959
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Ataxia-telangiectasia-like disorder 1 (ATLD1)
- Note
- DescriptionA rare disorder characterized by progressive cerebellar ataxia, dysarthria, abnormal eye movements, and absence of telangiectasia. ATLD patients show normal levels of total IgG, IgA and IgM, although there may be reduced levels of specific functional antibodies. At the cellular level, ATLD exhibits hypersensitivity to ionizing radiation and radioresistant DNA synthesis.
- See alsoMIM:604391
Natural variants in ATLD1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_089002 | 47 | A>V | in ATLD1 | |
VAR_008513 | 117 | N>S | in ATLD1; dbSNP:rs137852760 | |
VAR_089003 | 210 | W>C | in ATLD1 | |
VAR_089004 | 243 | W>R | in ATLD1; does not affect the DNA-binding and nuclease activities | |
VAR_089005 | 481 | T>K | in ATLD1 | |
VAR_089006 | 572-708 | missing | in ATLD1 | |
VAR_089007 | 633-708 | missing | in ATLD1 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_089002 | 47 | in ATLD1 | |||
Sequence: A → V | ||||||
Mutagenesis | 80 | Abolished interaction with NBN. | ||||
Sequence: R → A | ||||||
Mutagenesis | 87-117 | Abolished interaction with NBN. | ||||
Sequence: Missing | ||||||
Mutagenesis | 88 | Does not affect interaction with NBN. | ||||
Sequence: P → W | ||||||
Natural variant | VAR_011625 | 104 | in cancer; dbSNP:rs748434421 | |||
Sequence: S → C | ||||||
Natural variant | VAR_008513 | 117 | in ATLD1; dbSNP:rs137852760 | |||
Sequence: N → S | ||||||
Mutagenesis | 117 | Abolished interaction with NBN. | ||||
Sequence: N → L | ||||||
Mutagenesis | 121 | Abolished interaction with NBN. | ||||
Sequence: P → G | ||||||
Mutagenesis | 129-130 | Lacks the exonuclease activity. | ||||
Sequence: HD → LV | ||||||
Natural variant | VAR_011626 | 157 | in dbSNP:rs147771140 | |||
Sequence: M → V | ||||||
Natural variant | VAR_089003 | 210 | in ATLD1 | |||
Sequence: W → C | ||||||
Natural variant | VAR_036416 | 237 | in a breast cancer sample; somatic mutation | |||
Sequence: F → C | ||||||
Natural variant | VAR_089004 | 243 | in ATLD1; does not affect the DNA-binding and nuclease activities | |||
Sequence: W → R | ||||||
Mutagenesis | 255 | In 4KR mutant; strongly decreased SUMOylation; when associated with R-384, R-416 and R-467. | ||||
Sequence: K → R | ||||||
Mutagenesis | 282 | Abolished ufmylation. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_036417 | 302 | in a breast cancer sample; somatic mutation | |||
Sequence: H → Y | ||||||
Natural variant | VAR_025528 | 305 | in ovarian cancer; dbSNP:rs372000848 | |||
Sequence: R → W | ||||||
Mutagenesis | 339 | Abolished ubiquitination by RNF126; when associated with R-480. | ||||
Sequence: K → R | ||||||
Mutagenesis | 384 | In 4KR mutant; strongly decreased SUMOylation; when associated with R-255, R-416 and R-467. | ||||
Sequence: K → R | ||||||
Mutagenesis | 416 | In 4KR mutant; strongly decreased SUMOylation; when associated with R-255, R-384 and R-467. | ||||
Sequence: K → R | ||||||
Mutagenesis | 467 | In 4KR mutant; strongly decreased SUMOylation; when associated with R-255, R-384 and R-416. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_019288 | 468 | in dbSNP:rs1805367 | |||
Sequence: D → G | ||||||
Mutagenesis | 480 | Abolished ubiquitination by RNF126; when associated with R-339. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_089005 | 481 | in ATLD1 | |||
Sequence: T → K | ||||||
Natural variant | VAR_011627 | 503 | in cancer; dbSNP:rs774057024 | |||
Sequence: R → H | ||||||
Mutagenesis | 531 | Does not affect phosphorylation by ATM; when associated with A-590. | ||||
Sequence: S → A | ||||||
Mutagenesis | 570-594 | Abolished methylation, leading to decreased exonuclease activity. | ||||
Sequence: RGRGRGRRGGRGQNSASRGGSQRGR → KGKGKGKKGGKGQNSASKGGSQKGK | ||||||
Natural variant | VAR_011628 | 572 | in cancer; dbSNP:rs200085146 | |||
Sequence: R → Q | ||||||
Mutagenesis | 572-576 | Abolished interaction with C1QBP. | ||||
Sequence: RGRGR → QGRGQ | ||||||
Natural variant | VAR_089006 | 572-708 | in ATLD1 | |||
Sequence: Missing | ||||||
Mutagenesis | 590 | Does not affect phosphorylation by ATM; when associated with A-531. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_089007 | 633-708 | in ATLD1 | |||
Sequence: Missing | ||||||
Mutagenesis | 649 | Decreased phosphorylation; when associated with A-688. | ||||
Sequence: S → A | ||||||
Mutagenesis | 649 | Mimics phosphorylation; decreased ability to mediate DNA repair; when associated with D-688. | ||||
Sequence: S → D | ||||||
Mutagenesis | 673 | Abolished lactylation by CREBBP/CBP, leading to decreased DNA-binding. | ||||
Sequence: K → R | ||||||
Mutagenesis | 676-678 | Impaired phosphorylation by ATM, preventing interaction with C1QBP. | ||||
Sequence: SQS → AQA | ||||||
Mutagenesis | 688 | Decreased phosphorylation; when associated with A-649. | ||||
Sequence: S → A | ||||||
Mutagenesis | 688 | Mimics phosphorylation; decreased ability to mediate DNA repair; when associated with D-649. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_019289 | 698 | in dbSNP:rs1805362 | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,306 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 initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000138672 | 2-708 | UniProt | Double-strand break repair protein MRE11 | |||
Sequence: STADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 255 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 275 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 282 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1) | ||||
Sequence: K | |||||||
Cross-link | 339 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 384 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Cross-link | 416 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 467 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Cross-link | 480 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 558 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 570 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 572 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 574 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 576 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 577 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 580 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 587 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 592 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 594 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 619 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 619 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 625 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 641 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 649 | UniProt | Phosphoserine; by PLK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 673 | UniProt | N6-lactoyllysine | ||||
Sequence: K | |||||||
Modified residue | 676 | UniProt | Phosphoserine; by ATM | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 676 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 678 | UniProt | Phosphoserine; by ATM | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 688 | UniProt | Phosphoserine; by CDK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 688 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 689 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 701 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-649 by PLK1 primes for phosphorylation at Ser-688 by CK2, inhibiting recruitment of the MRN complex to DNA damage sites (PubMed:28512243).
Ubiquitination triggers interaction with UBQLN4, leading to MRE11 removal from chromatin and degradation by the proteasome (PubMed:30612738).
Ubiquitinated at Lys-339 and Lys-480 by RNF126 via 'Lys-27'- and 'Lys-29'-linked polyubiquitin chains, promoting the exonuclease activity of MRE11 (PubMed:36563124).
DeSUMOylated by SENP3 following removal from DNA double-strand breaks (DSBs) (PubMed:36050397).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:36577401).
As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites (PubMed:26215093).
Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (PubMed:10783165).
Found in a complex with TERF2 (PubMed:10888888).
Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo (PubMed:15456891, PubMed:15723659, PubMed:18469862).
Interacts with ATF2 (PubMed:15916964).
Interacts with EXD2 (PubMed:26807646).
Interacts with MRNIP (PubMed:27568553).
Interacts with SAMHD1; leading to stimulate 3'-5' exonuclease activity (PubMed:28834754, PubMed:29670289).
Interacts (when ubiquitinated) with UBQLN4 (via its UBA domain) (PubMed:30612738).
Interacts with CYREN (via XLF motif) (By similarity).
Interacts with GFI1; promoting methylation by PRMT1 (PubMed:29651020).
Interacts with DYNLL1; inhibiting the activity of MRE11 (PubMed:30464262, PubMed:37696958).
Interacts with C1QBP and RAD50; interaction takes place in absence of DNA damage to form the MRC (MRE11-RAD50-C1QBP) complex that inhibits the activity of MRE11 (PubMed:31353207).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P49959 | FANCD2 Q9BXW9 | 6 | EBI-396513, EBI-359343 | |
BINARY | P49959 | H2AX P16104 | 7 | EBI-396513, EBI-494830 | |
BINARY | P49959 | HTT P42858 | 5 | EBI-396513, EBI-466029 | |
BINARY | P49959 | MRE11 P49959 | 3 | EBI-396513, EBI-396513 | |
BINARY | P49959 | NBN O60934 | 5 | EBI-396513, EBI-494844 | |
XENO | P49959 | P03243-1 | 2 | EBI-396513, EBI-1927377 | |
BINARY | P49959 | RAD17 O75943 | 2 | EBI-396513, EBI-968231 | |
BINARY | P49959 | RBBP8 Q99708 | 3 | EBI-396513, EBI-745715 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 87-117 | Interaction with NBN | ||||
Sequence: RPVQFEILSDQSVNFGFSKFPWVNYQDGNLN | ||||||
Compositional bias | 507-528 | Basic and acidic residues | ||||
Sequence: TRQKNTNEEDDEVREAMTRARA | ||||||
Region | 507-540 | Disordered | ||||
Sequence: TRQKNTNEEDDEVREAMTRARALRSQSEESASAF | ||||||
Region | 556-614 | Disordered | ||||
Sequence: NDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSA | ||||||
Motif | 570-594 | GAR | ||||
Sequence: RGRGRGRRGGRGQNSASRGGSQRGR | ||||||
Compositional bias | 583-614 | Polar residues | ||||
Sequence: NSASRGGSQRGRADTGLETSTRSRNSKTAVSA | ||||||
Region | 651-708 | Disordered | ||||
Sequence: VEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR | ||||||
Compositional bias | 660-684 | Polar residues | ||||
Sequence: SKTDQRWSSTSSSKIMSQSQVSKGV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P49959-1
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
- Length708
- Mass (Da)80,593
- Last updated2001-09-26 v3
- ChecksumD94ABFBDDF6106AD
P49959-2
- Name2
- Differences from canonical
- 595-622: Missing
P49959-3
- Name3
- Differences from canonical
- 1-7: MSTADAL → MNRNISHQKG
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_057350 | 1-7 | in isoform 3 | |||
Sequence: MSTADAL → MNRNISHQKG | ||||||
Sequence conflict | 31 | in Ref. 1; AAC78721 | ||||
Sequence: V → A | ||||||
Compositional bias | 507-528 | Basic and acidic residues | ||||
Sequence: TRQKNTNEEDDEVREAMTRARA | ||||||
Compositional bias | 583-614 | Polar residues | ||||
Sequence: NSASRGGSQRGRADTGLETSTRSRNSKTAVSA | ||||||
Alternative sequence | VSP_003262 | 595-622 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 660-684 | Polar residues | ||||
Sequence: SKTDQRWSSTSSSKIMSQSQVSKGV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U37359 EMBL· GenBank· DDBJ | AAC78721.1 EMBL· GenBank· DDBJ | mRNA | ||
AF022778 EMBL· GenBank· DDBJ | AAD10197.1 EMBL· GenBank· DDBJ | mRNA | ||
AF073362 EMBL· GenBank· DDBJ | AAC36249.1 EMBL· GenBank· DDBJ | mRNA | ||
AF303395 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303379 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303380 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303381 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303382 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303383 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303384 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303385 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303386 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303387 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303388 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303389 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303390 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303391 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303392 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303393 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF303394 EMBL· GenBank· DDBJ | AAK18790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK095388 EMBL· GenBank· DDBJ | BAG53039.1 EMBL· GenBank· DDBJ | mRNA | ||
AY584241 EMBL· GenBank· DDBJ | AAS79320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP000765 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000786 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF455448 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC063458 EMBL· GenBank· DDBJ | AAH63458.1 EMBL· GenBank· DDBJ | mRNA |