Q9UPY3 · DICER_HUMAN
- ProteinEndoribonuclease Dicer
- GeneDICER1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1922 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64-71 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LNTGSGKT | ||||||
Binding site | 1316 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1395 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1398 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1705 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 1806 | Important for activity | ||||
Sequence: K | ||||||
Binding site | 1810 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1813 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndoribonuclease Dicer
- 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 accessionQ9UPY3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Pleuropulmonary blastoma (PPB)
- Note
- DescriptionA rare pediatric intrathoracic neoplasm. The tumor arises from the lung, pleura, or both, and appears to be purely mesenchymal in phenotype. It lacks malignant epithelial elements, a feature that distinguishes it from the classic adult-type pulmonary blastoma. It arises during fetal lung development and is often part of an inherited cancer syndrome. The tumor contain both epithelial and mesenchymal cells. Early in tumorigenesis, cysts form in lung airspaces, and these cysts are lined with benign-appearing epithelium. Mesenchymal cells susceptible to malignant transformation reside within the cyst walls and form a dense layer beneath the epithelial lining. In a subset of patients, overgrowth of the mesenchymal cells produces a sarcoma, a transition that is associated with a poorer prognosis. Some patients have multilocular cystic nephroma, a benign kidney tumor.
- See alsoMIM:601200
Natural variants in PPB
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_063150 | 1583 | L>R | in PPB; dbSNP:rs137852976 |
Goiter multinodular 1, with or without Sertoli-Leydig cell tumors (MNG1)
- Note
- DescriptionA common disorder characterized by nodular overgrowth of the thyroid gland. Some individuals may also develop Sertoli-Leydig cell tumors, usually of the ovary.
- See alsoMIM:138800
Natural variants in MNG1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_065301 | 839 | S>F | in MNG1; dbSNP:rs387906934 |
Rhabdomyosarcoma, embryonal, 2 (RMSE2)
- Note
- DescriptionA form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas.
- See alsoMIM:180295
Global developmental delay, lung cysts, overgrowth, and Wilms tumor (GLOW)
- Note
- DescriptionA disease characterized by the association of congenital nephromegaly, bilateral Wilms tumor, somatic overgrowth, developmental delay, macrocephaly, and bilateral lung cysts.
- See alsoMIM:618272
Natural variants in GLOW
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081918 | 1709 | D>Y | in GLOW; somatic mutation | |
VAR_081919 | 1713 | D>V | in GLOW; somatic mutation |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_081917 | 435 | found in Wilms tumor from a patient with GLOW syndrome; uncertain significance; somatic mutation | |||
Sequence: P → L | ||||||
Natural variant | VAR_065301 | 839 | in MNG1; dbSNP:rs387906934 | |||
Sequence: S → F | ||||||
Mutagenesis | 960 | 2-fold decrease in activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 971 | 10-fold decrease in activity; when associated with Y-972. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 972 | 10-fold decrease in activity; when associated with Y-971. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 1036 | 5-fold decrease in activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 1313 | No effect on activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 1320 | Decreased activity. Loss of activity; when associated with D-1709. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1340 | No effect on activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 1444 | Decreased activity. Loss of activity; when associated with E-1813. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_063150 | 1583 | in PPB; dbSNP:rs137852976 | |||
Sequence: L → R | ||||||
Mutagenesis | 1702 | No effect on activity. | ||||
Sequence: Q → A | ||||||
Natural variant | VAR_067091 | 1705 | in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity | |||
Sequence: E → K | ||||||
Natural variant | VAR_067092 | 1709 | in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity | |||
Sequence: D → E | ||||||
Natural variant | VAR_067093 | 1709 | in non-epithelial ovarian tumor; somatic mutation; dbSNP:rs1555366979 | |||
Sequence: D → G | ||||||
Natural variant | VAR_067094 | 1709 | in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity | |||
Sequence: D → N | ||||||
Natural variant | VAR_081918 | 1709 | in GLOW; somatic mutation | |||
Sequence: D → Y | ||||||
Mutagenesis | 1709 | Decreased activity. Loss of activity; when associated with D-1320. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_081919 | 1713 | in GLOW; somatic mutation | |||
Sequence: D → V | ||||||
Mutagenesis | 1729 | No effect on activity. | ||||
Sequence: P → E | ||||||
Natural variant | VAR_067095 | 1810 | in non-epithelial ovarian tumor; somatic mutation | |||
Sequence: D → H | ||||||
Natural variant | VAR_067096 | 1810 | in non-epithelial ovarian tumor; somatic mutation; dbSNP:rs775912475 | |||
Sequence: D → N | ||||||
Natural variant | VAR_067097 | 1810 | in non-epithelial ovarian tumor; somatic mutation | |||
Sequence: D → Y | ||||||
Natural variant | VAR_067098 | 1813 | in non-epithelial ovarian tumor; somatic mutation | |||
Sequence: E → G | ||||||
Natural variant | VAR_067099 | 1813 | in non-epithelial ovarian tumor; somatic mutation | |||
Sequence: E → K | ||||||
Natural variant | VAR_067100 | 1813 | in non-epithelial ovarian tumor; somatic mutation | |||
Sequence: E → Q | ||||||
Mutagenesis | 1813 | Decreased activity. Loss of activity; when associated with E-1444. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_081920 | 1898 | found in Wilms tumor from a patient with GLOW syndrome; uncertain significance; somatic mutation | |||
Sequence: R → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,362 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000180470 | 1-1922 | UniProt | Endoribonuclease Dicer | |||
Sequence: MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS | |||||||
Modified residue | 413 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 415 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 643 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1015 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1016 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1016 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1160 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1438 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1460 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1468 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1468 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1470 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1470 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1479 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1852 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1868 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1868 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1922 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts (via Dicer dsRNA-binding fold domain) with ALOX5 (via PLAT domain); this interaction enhances arachidonate 5-lipoxygenase activity and modifies the miRNA precursor processing activity of DICER1 (PubMed:19022417).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-227 | Helicase ATP-binding | ||||
Sequence: LLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLE | ||||||
Motif | 175-178 | DECH box | ||||
Sequence: DECH | ||||||
Region | 256-595 | Required for interaction with PRKRA and TARBP2 | ||||
Sequence: DCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVD | ||||||
Region | 409-433 | Disordered | ||||
Sequence: YVSWSDSEDDDEDEEIEEKEKPETN | ||||||
Compositional bias | 412-427 | Acidic residues | ||||
Sequence: WSDSEDDDEDEEIEEK | ||||||
Domain | 433-602 | Helicase C-terminal | ||||
Sequence: NFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDID | ||||||
Domain | 630-722 | Dicer dsRNA-binding fold | ||||
Sequence: AIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKY | ||||||
Domain | 895-1042 | PAZ | ||||
Sequence: KFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHP | ||||||
Domain | 1276-1403 | RNase III 1 | ||||
Sequence: DSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMT | ||||||
Domain | 1666-1824 | RNase III 2 | ||||
Sequence: FENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSG | ||||||
Domain | 1849-1914 | DRBM | ||||
Sequence: VPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKA |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9UPY3-1
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
- Length1,922
- Mass (Da)218,682
- Last updated2009-09-01 v3
- Checksum9452B96A601D4551
Q9UPY3-2
- Name2
- Synonymst-Dicer
- Differences from canonical
- 1789-1922: LRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS → KSFLQMYPVPLCENCLKWNQKLPNLARLRELTTGRSESLWK
Q9UPY3-3
- Name3
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6Q8PFV4 | A0A6Q8PFV4_HUMAN | DICER1 | 1090 | ||
A0A6Q8PH99 | A0A6Q8PH99_HUMAN | DICER1 | 522 | ||
A0A6Q8PHG6 | A0A6Q8PHG6_HUMAN | DICER1 | 563 | ||
H0YJZ6 | H0YJZ6_HUMAN | DICER1 | 1715 | ||
F6SZ09 | F6SZ09_HUMAN | DICER1 | 96 | ||
A0A7I2YBM0 | A0A7I2YBM0_HUMAN | DICER1 | 1802 | ||
Q5D0K5 | Q5D0K5_HUMAN | DICER1 | 70 | ||
A0A8Q3WLH6 | A0A8Q3WLH6_HUMAN | DICER1 | 133 | ||
A0A8Q3WLH8 | A0A8Q3WLH8_HUMAN | DICER1 | 1868 | ||
A0A8Q3WLJ5 | A0A8Q3WLJ5_HUMAN | DICER1 | 1789 | ||
A0A8Q3SJI0 | A0A8Q3SJI0_HUMAN | DICER1 | 1790 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055341 | 1-13 | in isoform 3 | |||
Sequence: MKSPALQPLSMAG → MLAWESDHFLRIL | ||||||
Alternative sequence | VSP_055342 | 14-1115 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 75-90 | in Ref. 1; BAA78691 | ||||
Sequence: VLLTKELSYQIRGDFS → STTLLKSCLYLDLGETSA | ||||||
Sequence conflict | 189 | in Ref. 1; BAA78691 | ||||
Sequence: I → F | ||||||
Sequence conflict | 195 | in Ref. 1; BAA78691 | ||||
Sequence: N → I | ||||||
Sequence conflict | 214 | in Ref. 1; BAA78691 | ||||
Sequence: C → W | ||||||
Sequence conflict | 218 | in Ref. 1; BAA78691 | ||||
Sequence: E → D | ||||||
Sequence conflict | 223 | in Ref. 1; BAA78691 | ||||
Sequence: I → F | ||||||
Sequence conflict | 393-394 | in Ref. 1; BAA78691 | ||||
Sequence: QQ → HS | ||||||
Compositional bias | 412-427 | Acidic residues | ||||
Sequence: WSDSEDDDEDEEIEEK | ||||||
Sequence conflict | 492-493 | in Ref. 1; BAA78691 | ||||
Sequence: KQ → NT | ||||||
Sequence conflict | 609 | in Ref. 1; BAA78691 | ||||
Sequence: D → H | ||||||
Alternative sequence | VSP_042832 | 1789-1922 | in isoform 2 | |||
Sequence: LRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS → KSFLQMYPVPLCENCLKWNQKLPNLARLRELTTGRSESLWK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB028449 EMBL· GenBank· DDBJ | BAA78691.1 EMBL· GenBank· DDBJ | mRNA | ||
HM595745 EMBL· GenBank· DDBJ | ADK25182.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ132261 EMBL· GenBank· DDBJ | CAB38857.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB023145 EMBL· GenBank· DDBJ | BAA76772.2 EMBL· GenBank· DDBJ | mRNA | ||
AK091513 EMBL· GenBank· DDBJ | BAG52376.1 EMBL· GenBank· DDBJ | mRNA | ||
AL356017 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL390254 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471061 EMBL· GenBank· DDBJ | EAW81596.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC150287 EMBL· GenBank· DDBJ | AAI50288.1 EMBL· GenBank· DDBJ | mRNA |