O96028 · NSD2_HUMAN
- ProteinHistone-lysine N-methyltransferase NSD2
- GeneNSD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308).
Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308).
However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity).
By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617).
In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation (By similarity).
During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes (By similarity).
Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation (PubMed:29728617).
During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation (By similarity).
During B-cell development, required for the generation of the B1 lineage (By similarity).
During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response (By similarity).
Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation (By similarity).
By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA (By similarity).
Isoform 1
Isoform 4
Methylation of histone H3 at 'Lys-27' is controversial (PubMed:18172012, PubMed:22099308).
Mono-, di- or tri-methylates histone H3 at 'Lys-27' (H3K27me, H3K27me2 and H3K27me3) (PubMed:18172012).
Does not methylate histone H3 at 'Lys-27' (PubMed:22099308).
May act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment (PubMed:11152655, PubMed:18172012).
Catalytic activity
- L-lysyl36-[histone H3] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl36-[histone H3] + S-adenosyl-L-homocysteine
Features
Showing features for dna binding, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 453-521 | HMG box | ||||
Sequence: KGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNV | ||||||
Binding site | 1016 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1018 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1026 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1026 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1032 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1041 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1046 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1052 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1075 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 1115-1118 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: THFY | ||||||
Binding site | 1141-1142 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: NH | ||||||
Binding site | 1144 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1186 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1191 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1192 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1193 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1198 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase NSD2
- 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 accessionO96028
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
In B-cells, localizes to Ig heavy chain switch region during class switch recombination (By similarity).
Isoform 1
Isoform 3
Isoform 4
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Rauch-Steindl syndrome (RAUST)
- Note
- DescriptionAn autosomal dominant disorder characterized by poor pre- and postnatal growth, facial dysmorphism, and variable developmental delay with delayed motor and speech acquisition and impaired intellectual. Other features may include hypotonia and behavioral abnormalities.
- See alsoMIM:619695
Natural variants in RAUST
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086787 | 600-1365 | missing | in RAUST | |
VAR_086788 | 720-1365 | missing | in RAUST | |
VAR_086789 | 755-1365 | missing | in RAUST | |
VAR_086790 | 869 | C>Y | in RAUST; not changed histone methyltransferase activity H3-K36 specific | |
VAR_086791 | 895 | P>L | in RAUST; decreased histone methyltransferase activity H3-K36 specific | |
VAR_086792 | 935-1365 | missing | in RAUST | |
VAR_086793 | 1019 | K>R | in RAUST; decreased histone methyltransferase activity H3-K36 specific | |
VAR_086794 | 1091 | E>K | in RAUST | |
VAR_086795 | 1137 | S>F | in RAUST; decreased histone methyltransferase activity H3-K36 specific | |
VAR_086796 | 1138-1365 | missing | in RAUST |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_086787 | 600-1365 | in RAUST | |||
Sequence: Missing | ||||||
Natural variant | VAR_086788 | 720-1365 | in RAUST | |||
Sequence: Missing | ||||||
Natural variant | VAR_086789 | 755-1365 | in RAUST | |||
Sequence: Missing | ||||||
Natural variant | VAR_086790 | 869 | in RAUST; not changed histone methyltransferase activity H3-K36 specific | |||
Sequence: C → Y | ||||||
Natural variant | VAR_086791 | 895 | in RAUST; decreased histone methyltransferase activity H3-K36 specific | |||
Sequence: P → L | ||||||
Natural variant | VAR_086792 | 935-1365 | in RAUST | |||
Sequence: Missing | ||||||
Natural variant | VAR_086793 | 1019 | in RAUST; decreased histone methyltransferase activity H3-K36 specific | |||
Sequence: K → R | ||||||
Natural variant | VAR_086794 | 1091 | in RAUST | |||
Sequence: E → K | ||||||
Mutagenesis | 1092 | Loss of methyltransferase activity. Reduces levels of H3K36me2 in preadipocytes; when associated with A-1179. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_086795 | 1137 | in RAUST; decreased histone methyltransferase activity H3-K36 specific | |||
Sequence: S → F | ||||||
Natural variant | VAR_086796 | 1138-1365 | in RAUST | |||
Sequence: Missing | ||||||
Mutagenesis | 1142 | Reduces levels of H3K36me2 in preadipocytes; when associated with A-1179. | ||||
Sequence: H → G | ||||||
Mutagenesis | 1179 | Loss of methyltransferase activity. Reduces levels of H3K36me2 in preadipocytes; when associated with A-1092 or G-1142. | ||||
Sequence: Y → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,463 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000259519 | 1-1365 | UniProt | Histone-lysine N-methyltransferase NSD2 | |||
Sequence: MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKGKMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKNALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSGFLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGRSYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 30 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 110 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 114 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 114 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 121 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 172 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 376 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 421 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 422 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 422 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 544 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 604 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 614 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1316 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O96028 | AR P10275 | 5 | EBI-2693298, EBI-608057 | |
BINARY | O96028 | HORMAD2 Q8N7B1 | 3 | EBI-2693298, EBI-13346145 | |
BINARY | O96028 | MDC1 Q14676 | 3 | EBI-2693298, EBI-495644 | |
BINARY | O96028 | PLEKHF2 Q9H8W4 | 3 | EBI-2693298, EBI-742388 | |
BINARY | O96028-1 | MDC1 Q14676 | 3 | EBI-15910280, EBI-495644 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 149-170 | Disordered | ||||
Sequence: ADVSQSEENGQKPENKARRNRK | ||||||
Domain | 222-286 | PWWP 1 | ||||
Sequence: VGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEG | ||||||
Region | 376-455 | Disordered | ||||
Sequence: SSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGD | ||||||
Compositional bias | 385-408 | Basic and acidic residues | ||||
Sequence: ENPKSVREECIPMKRRRRAKLCSS | ||||||
Region | 516-658 | Disordered | ||||
Sequence: EDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKS | ||||||
Compositional bias | 519-566 | Basic and acidic residues | ||||
Sequence: GNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKT | ||||||
Compositional bias | 567-590 | Polar residues | ||||
Sequence: ARTSSYKAMEAASSLKSQAATKNL | ||||||
Compositional bias | 602-630 | Polar residues | ||||
Sequence: RASTAASSALGFSKSSSPSASLTENEVSD | ||||||
Compositional bias | 642-658 | Polar residues | ||||
Sequence: ESADETQTEVSVSSKKS | ||||||
Zinc finger | 667-713 | PHD-type 1 | ||||
Sequence: EYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASG | ||||||
Zinc finger | 714-770 | PHD-type 2 | ||||
Sequence: IHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHAS | ||||||
Zinc finger | 831-875 | PHD-type 3 | ||||
Sequence: VSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAG | ||||||
Domain | 880-942 | PWWP 2 | ||||
Sequence: FQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEG | ||||||
Domain | 1011-1061 | AWS | ||||
Sequence: SEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQ | ||||||
Domain | 1063-1180 | SET | ||||
Sequence: PETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYN | ||||||
Domain | 1187-1203 | Post-SET | ||||
Sequence: EKTVCRCGASNCSGFLG | ||||||
Region | 1207-1232 | Disordered | ||||
Sequence: KTSTTLSSEEKGKKTKKKTRRRRAKG | ||||||
Zinc finger | 1239-1286 | PHD-type 4; atypical | ||||
Sequence: EDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCD | ||||||
Region | 1333-1365 | Disordered | ||||
Sequence: VRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
O96028-1
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
- SynonymsMMSET type II
- Length1,365
- Mass (Da)152,258
- Last updated1999-05-01 v1
- Checksum7B3128E1FA893AAA
O96028-2
- Name2
O96028-3
- Name3
- SynonymsMMSET type I
O96028-4
- Name4
- SynonymsRE-IIBP, IL-5 promoter REII-region-binding protein
- Differences from canonical
- 1-781: Missing
O96028-5
- Name5
O96028-6
- Name6
O96028-7
- Name7
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6RIS1 | D6RIS1_HUMAN | NSD2 | 199 | ||
D6RFE7 | D6RFE7_HUMAN | NSD2 | 37 | ||
D6R9V2 | D6R9V2_HUMAN | NSD2 | 392 | ||
H0Y9L4 | H0Y9L4_HUMAN | NSD2 | 163 | ||
H0Y9U6 | H0Y9U6_HUMAN | NSD2 | 284 | ||
A0A7P0P278 | A0A7P0P278_HUMAN | NSD2 | 629 | ||
A0A7I2YQS5 | A0A7I2YQS5_HUMAN | NSD2 | 800 | ||
A0A7I2V2S2 | A0A7I2V2S2_HUMAN | NSD2 | 269 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_021414 | 1-652 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021413 | 1-781 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 26 | In isoform O96028-2; in Ref. 7; BAA83042 and 11; AAI52413 | ||||
Sequence: M → V | ||||||
Sequence conflict | 210 | in Ref. 5; AAU09264 | ||||
Sequence: T → A | ||||||
Alternative sequence | VSP_021415 | 255-273 | in isoform 7 | |||
Sequence: QKKSARQYHVQFFGDAPER → IFKSKKFEHLKTSQIVLKD | ||||||
Alternative sequence | VSP_021416 | 274-1365 | in isoform 7 | |||
Sequence: Missing | ||||||
Compositional bias | 385-408 | Basic and acidic residues | ||||
Sequence: ENPKSVREECIPMKRRRRAKLCSS | ||||||
Alternative sequence | VSP_021417 | 472-484 | in isoform 6 | |||
Sequence: VAEHPDASGEEIE → STKLCFMLASFRI | ||||||
Alternative sequence | VSP_021418 | 485-1365 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 519-566 | Basic and acidic residues | ||||
Sequence: GNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKT | ||||||
Compositional bias | 567-590 | Polar residues | ||||
Sequence: ARTSSYKAMEAASSLKSQAATKNL | ||||||
Compositional bias | 602-630 | Polar residues | ||||
Sequence: RASTAASSALGFSKSSSPSASLTENEVSD | ||||||
Alternative sequence | VSP_021419 | 628-647 | in isoform 3 | |||
Sequence: VSDSPGDEPSESPYESADET → LLWEPTPVKLDLNPAALYCT | ||||||
Alternative sequence | VSP_021420 | 629 | in isoform 5 | |||
Sequence: S → K | ||||||
Alternative sequence | VSP_021421 | 630-1365 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 642-658 | Polar residues | ||||
Sequence: ESADETQTEVSVSSKKS | ||||||
Alternative sequence | VSP_021422 | 648-1365 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021423 | 653-712 | in isoform 2 | |||
Sequence: VSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECAS → MAGSFCWRMLGLVSKVGNRARCFSSMAASEEELLDFSGSELQFNSCSLHLSLHPFFNFLL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF071593 EMBL· GenBank· DDBJ | AAC24150.1 EMBL· GenBank· DDBJ | mRNA | ||
AF071594 EMBL· GenBank· DDBJ | AAC24151.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083386 EMBL· GenBank· DDBJ | AAD19343.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083387 EMBL· GenBank· DDBJ | AAD21770.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083388 EMBL· GenBank· DDBJ | AAD21771.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083389 EMBL· GenBank· DDBJ | AAD19344.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083390 EMBL· GenBank· DDBJ | AAD19345.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083391 EMBL· GenBank· DDBJ | AAD19346.1 EMBL· GenBank· DDBJ | mRNA | ||
AF178206 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178199 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178198 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178202 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178204 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178205 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178203 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178201 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178200 EMBL· GenBank· DDBJ | AAF23369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178219 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178198 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178199 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178200 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178202 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178204 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178207 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178216 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178215 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178214 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178213 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178212 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178211 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178210 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178209 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178208 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178218 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178217 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178205 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178203 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF178201 EMBL· GenBank· DDBJ | AAF23370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF330040 EMBL· GenBank· DDBJ | AAK00344.1 EMBL· GenBank· DDBJ | mRNA | ||
AY694128 EMBL· GenBank· DDBJ | AAU09264.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ007042 EMBL· GenBank· DDBJ | CAB45386.1 EMBL· GenBank· DDBJ | mRNA | ||
AB029013 EMBL· GenBank· DDBJ | BAA83042.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK289697 EMBL· GenBank· DDBJ | BAF82386.1 EMBL· GenBank· DDBJ | mRNA | ||
AC105448 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL132868 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471131 EMBL· GenBank· DDBJ | EAW82548.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82552.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82557.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82553.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82556.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC052254 EMBL· GenBank· DDBJ | AAH52254.1 EMBL· GenBank· DDBJ | mRNA | ||
BC070176 EMBL· GenBank· DDBJ | AAH70176.1 EMBL· GenBank· DDBJ | mRNA | ||
BC094825 EMBL· GenBank· DDBJ | AAH94825.2 EMBL· GenBank· DDBJ | mRNA | ||
BC141815 EMBL· GenBank· DDBJ | AAI41816.1 EMBL· GenBank· DDBJ | mRNA | ||
BC152412 EMBL· GenBank· DDBJ | AAI52413.1 EMBL· GenBank· DDBJ | mRNA |