Q8NHM5 · KDM2B_HUMAN
- ProteinLysine-specific demethylase 2B
- GeneKDM2B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36' (PubMed:16362057, PubMed:17994099, PubMed:26237645).
Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation (PubMed:16362057, PubMed:17994099).
May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex (Probable)
Catalytic activity
- 2 2-oxoglutarate + N6,N6-dimethyl-L-lysyl36-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl36-[histone H3] + 2 succinate
2 CHEBI:16810 + RHEA-COMP:9787 CHEBI:61976 Position: 36+ 2 CHEBI:15379 = 2 CHEBI:16526 + 2 CHEBI:16842 + RHEA-COMP:9785 CHEBI:29969 Position: 36+ 2 CHEBI:30031
Cofactor
Activity regulation
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 239 | substrate | ||||
Sequence: T | ||||||
Binding site | 242 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 244 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 259 | substrate | ||||
Sequence: K | ||||||
Binding site | 314 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 613 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 616 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 619 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 624 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 627 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 630 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 646 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 651 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 662 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 665 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 688 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 691 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 696 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 699 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 719 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 722 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLysine-specific demethylase 2B
- 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 accessionQ8NHM5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1064 | Increased interaction with UBB. | ||||
Sequence: V → W | ||||||
Mutagenesis | 1069 | Decreased ininteraction with UBB. | ||||
Sequence: V → A | ||||||
Mutagenesis | 1072 | Increased interaction with UBB. | ||||
Sequence: A → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,258 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000119853 | 1-1336 | UniProt | Lysine-specific demethylase 2B | |||
Sequence: MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQRPIDRQRYDENEDLSDVEEIVSVRGFSLEEKLRSQLYQGDFVHAMEGKDFNYEYVQREALRVPLIFREKDGLGIKMPDPDFTVRDVKLLVGSRRLVDVMDVNTQKGTEMSMSQFVRYYETPEAQRDKLYNVISLEFSHTKLEHLVKRPTVVDLVDWVDNMWPQHLKEKQTEATNAIAEMKYPKVKKYCLMSVKGCFTDFHIDFGGTSVWYHVFRGGKIFWLIPPTLHNLALYEEWVLSGKQSDIFLGDRVERCQRIELKQGYTFFIPSGWIHAVYTPVDSLVFGGNILHSFNVPMQLRIYEIEDRTRVQPKFRYPFYYEMCWYVLERYVYCVTQRSHLTQEYQRESMLIDAPRKPSIDGFSSDSWLEMEEEACDQQPQEEEEKDEEGEGRDRAPKPPTDGSTSPTSTPSEDQEALGKKPKAPALRFLKRTLSNESEESVKSTTLAVDYPKTPTGSPATEVSAKWTHLTEFELKGLKALVEKLESLPENKKCVPEGIEDPQALLEGVKNVLKEHADDDPSLAITGVPVVTWPKKTPKNRAVGRPKGKLGPASAVKLAANRTTAGARRRRTRCRKCEACLRTECGECHFCKDMKKFGGPGRMKQSCIMRQCIAPVLPHTAVCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKIKESEGVVNDELPNCWECPKCNHAGKTGKQKRGPGFKYASNLPGSLLKEQKMNRDNKEGQEPAKRRSECEEAPRRRSDEHSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSGRKRASSLQTSPGSSSHLSPRPPLGSSLSPWWRSSLTYFQQQLKPGKEDKLFRKKRRSWKNAEDRMALANKPLRRFKQEPEDELPEAPPKTRESDHSRSSSPTAGPSTEGAEGPEEKKKVKMRRKRRLPNKELSRELSKELNHEIQRTENSLANENQQPIKSEPESEGEEPKRPPGICERPHRFSKGLNGTPRELRHQLGPSLRSPPRVISRPPPSVSPPKCIQMERHVIRPPPISPPPDSLPLDDGAAHVMHREVWMAVFSYLSHQDLCVCMRVCRTWNRWCCDKRLWTRIDLNHCKSITPLMLSGIIRRQPVSLDLSWTNISKKQLSWLINRLPGLRDLVLSGCSWIAVSALCSSSCPLLRTLDVQWVEGLKDAQMRDLLSPPTDNRPGQMDNRSKLRNIVELRLAGLDITDASLRLIIRHMPLLSKLHLSYCNHVTDQSINLLTAVGTTTRDSLTEINLSDCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS | |||||||
Modified residue | 57 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 443 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 445 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 474 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 474 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 477 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 477 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 480 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 493 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 493 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 495 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 497 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 497 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 746 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 768 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 824 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 857 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 890 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 914 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 951 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 964 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 975 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 975 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 979 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 979 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1015 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1018 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1018 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1029 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1031 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1031 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1049 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
The heterodimeric KDM2B-SKP1 complex interacts with the PCGF1-BCORL1 heterodimeric complex to form a homotetrameric polycomb repression complex 1 (PRC1.1) (PubMed:27568929).
Directly interacts with CUL1. The SKP1-KDM2B complex interacts with UBB (PubMed:30033217).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NHM5 | BCOR Q6W2J9 | 5 | EBI-3955564, EBI-950027 | |
BINARY | Q8NHM5 | SKP1 P63208 | 8 | EBI-3955564, EBI-307486 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, zinc finger, coiled coil, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MAGPQMGGSAEDHPPRKRHAAEKQK | ||||||
Domain | 178-346 | JmjC | ||||
Sequence: FSHTKLEHLVKRPTVVDLVDWVDNMWPQHLKEKQTEATNAIAEMKYPKVKKYCLMSVKGCFTDFHIDFGGTSVWYHVFRGGKIFWLIPPTLHNLALYEEWVLSGKQSDIFLGDRVERCQRIELKQGYTFFIPSGWIHAVYTPVDSLVFGGNILHSFNVPMQLRIYEIED | ||||||
Compositional bias | 410-428 | Acidic residues | ||||
Sequence: MEEEACDQQPQEEEEKDEE | ||||||
Region | 410-465 | Disordered | ||||
Sequence: MEEEACDQQPQEEEEKDEEGEGRDRAPKPPTDGSTSPTSTPSEDQEALGKKPKAPA | ||||||
Compositional bias | 440-454 | Polar residues | ||||
Sequence: TDGSTSPTSTPSEDQ | ||||||
Zinc finger | 606-652 | CXXC-type | ||||
Sequence: ARRRRTRCRKCEACLRTECGECHFCKDMKKFGGPGRMKQSCIMRQCI | ||||||
Zinc finger | 659-725 | PHD-type | ||||
Sequence: TAVCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKIKESEGVVNDELPNCWECPKCNHA | ||||||
Region | 727-843 | Disordered | ||||
Sequence: KTGKQKRGPGFKYASNLPGSLLKEQKMNRDNKEGQEPAKRRSECEEAPRRRSDEHSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSGRKRASSLQTSPGSSSHLSPRPPLGSSLSP | ||||||
Compositional bias | 751-814 | Basic and acidic residues | ||||
Sequence: QKMNRDNKEGQEPAKRRSECEEAPRRRSDEHSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSG | ||||||
Compositional bias | 815-843 | Polar residues | ||||
Sequence: RKRASSLQTSPGSSSHLSPRPPLGSSLSP | ||||||
Region | 855-1034 | Disordered | ||||
Sequence: QLKPGKEDKLFRKKRRSWKNAEDRMALANKPLRRFKQEPEDELPEAPPKTRESDHSRSSSPTAGPSTEGAEGPEEKKKVKMRRKRRLPNKELSRELSKELNHEIQRTENSLANENQQPIKSEPESEGEEPKRPPGICERPHRFSKGLNGTPRELRHQLGPSLRSPPRVISRPPPSVSPPK | ||||||
Compositional bias | 868-910 | Basic and acidic residues | ||||
Sequence: KRRSWKNAEDRMALANKPLRRFKQEPEDELPEAPPKTRESDHS | ||||||
Compositional bias | 942-959 | Basic and acidic residues | ||||
Sequence: PNKELSRELSKELNHEIQ | ||||||
Coiled coil | 943-971 | |||||
Sequence: NKELSRELSKELNHEIQRTENSLANENQQ | ||||||
Compositional bias | 960-974 | Polar residues | ||||
Sequence: RTENSLANENQQPIK | ||||||
Compositional bias | 975-1003 | Basic and acidic residues | ||||
Sequence: SEPESEGEEPKRPPGICERPHRFSKGLNG | ||||||
Domain | 1059-1105 | F-box | ||||
Sequence: DGAAHVMHREVWMAVFSYLSHQDLCVCMRVCRTWNRWCCDKRLWTRI | ||||||
Repeat | 1093-1120 | LRR 1 | ||||
Sequence: NRWCCDKRLWTRIDLNHCKSITPLMLSG | ||||||
Repeat | 1133-1154 | LRR 2 | ||||
Sequence: WTNISKKQLSWLINRLPGLRDL | ||||||
Repeat | 1156-1182 | LRR 3 | ||||
Sequence: LSGCSWIAVSALCSSSCPLLRTLDVQW | ||||||
Repeat | 1222-1247 | LRR 4 | ||||
Sequence: GLDITDASLRLIIRHMPLLSKLHLSY | ||||||
Repeat | 1248-1277 | LRR 5 | ||||
Sequence: CNHVTDQSINLLTAVGTTTRDSLTEINLSD | ||||||
Repeat | 1278-1302 | LRR 6 | ||||
Sequence: CNKVTDQCLSFFKRCGNICHIDLRY | ||||||
Repeat | 1303-1336 | LRR 7 | ||||
Sequence: CKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS |
Domain
It is also required for repression of ribosomal RNA genes (PubMed:17994099).
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q8NHM5-1
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
- Length1,336
- Mass (Da)152,615
- Last updated2002-10-01 v1
- Checksum3A1A17B8EA9EA953
Q8NHM5-2
- Name2
- Differences from canonical
- 730-730: K → KAYK
- 1277-1336: DCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS → ASLLGRVFGLQFWGICEPQARKNAGWA
Q8NHM5-3
- Name3
- Differences from canonical
- 856-868: LKPGKEDKLFRKK → Q
- 1204-1204: G → GPG
Q8NHM5-4
- Name4
- Differences from canonical
- 1-42: MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQ → MEAEKDSGRRL
- 818-855: Missing
- 1320-1336: VSVQFGQVEEKLLQKLS → SFQGRSCSTTRLGDE
Q8NHM5-5
- Name5
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WBN2 | F8WBN2_HUMAN | KDM2B | 510 | ||
S4R3G4 | S4R3G4_HUMAN | KDM2B | 507 | ||
F5GXC2 | F5GXC2_HUMAN | KDM2B | 180 | ||
F5GXW2 | F5GXW2_HUMAN | KDM2B | 123 | ||
F5H6N6 | F5H6N6_HUMAN | KDM2B | 154 | ||
F5H7T7 | F5H7T7_HUMAN | KDM2B | 97 | ||
F5H4X4 | F5H4X4_HUMAN | KDM2B | 125 | ||
F5H5W7 | F5H5W7_HUMAN | KDM2B | 41 | ||
F5H4A7 | F5H4A7_HUMAN | KDM2B | 171 | ||
A0A0C4DGG3 | A0A0C4DGG3_HUMAN | KDM2B | 704 | ||
F5H0A1 | F5H0A1_HUMAN | KDM2B | 104 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043146 | 1-42 | in isoform 4 | |||
Sequence: MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQ → MEAEKDSGRRL | ||||||
Alternative sequence | VSP_057394 | 1-117 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 410-428 | Acidic residues | ||||
Sequence: MEEEACDQQPQEEEEKDEE | ||||||
Compositional bias | 440-454 | Polar residues | ||||
Sequence: TDGSTSPTSTPSEDQ | ||||||
Alternative sequence | VSP_057395 | 654-676 | in isoform 5 | |||
Sequence: PVLPHTAVCLVCGEAGKEDTVEE → TAIRSLISACPSSNAVETSVILT | ||||||
Alternative sequence | VSP_057396 | 677-1336 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011340 | 730 | in isoform 2 | |||
Sequence: K → KAYK | ||||||
Compositional bias | 751-814 | Basic and acidic residues | ||||
Sequence: QKMNRDNKEGQEPAKRRSECEEAPRRRSDEHSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSG | ||||||
Compositional bias | 815-843 | Polar residues | ||||
Sequence: RKRASSLQTSPGSSSHLSPRPPLGSSLSP | ||||||
Alternative sequence | VSP_043147 | 818-855 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017475 | 856-868 | in isoform 3 | |||
Sequence: LKPGKEDKLFRKK → Q | ||||||
Sequence conflict | 864 | in Ref. 6; BAC11159 | ||||
Sequence: L → F | ||||||
Compositional bias | 868-910 | Basic and acidic residues | ||||
Sequence: KRRSWKNAEDRMALANKPLRRFKQEPEDELPEAPPKTRESDHS | ||||||
Compositional bias | 942-959 | Basic and acidic residues | ||||
Sequence: PNKELSRELSKELNHEIQ | ||||||
Compositional bias | 960-974 | Polar residues | ||||
Sequence: RTENSLANENQQPIK | ||||||
Compositional bias | 975-1003 | Basic and acidic residues | ||||
Sequence: SEPESEGEEPKRPPGICERPHRFSKGLNG | ||||||
Alternative sequence | VSP_017476 | 1204 | in isoform 3 | |||
Sequence: G → GPG | ||||||
Sequence conflict | 1226 | in Ref. 6; BAC11159 | ||||
Sequence: T → R | ||||||
Alternative sequence | VSP_011341 | 1277-1336 | in isoform 2 | |||
Sequence: DCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS → ASLLGRVFGLQFWGICEPQARKNAGWA | ||||||
Sequence conflict | 1295 | in Ref. 6; BAC11159 | ||||
Sequence: I → T | ||||||
Alternative sequence | VSP_043148 | 1320-1336 | in isoform 4 | |||
Sequence: VSVQFGQVEEKLLQKLS → SFQGRSCSTTRLGDE | ||||||
Sequence conflict | 1334 | in Ref. 6; BAC11159 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ459424 EMBL· GenBank· DDBJ | CAD30700.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027440 EMBL· GenBank· DDBJ | BAB55112.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK027692 EMBL· GenBank· DDBJ | BAB55301.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK074718 EMBL· GenBank· DDBJ | BAC11159.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK127328 EMBL· GenBank· DDBJ | BAG54483.1 EMBL· GenBank· DDBJ | mRNA | ||
AC048337 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC073650 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC145422 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877509 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC008735 EMBL· GenBank· DDBJ | AAH08735.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC115379 EMBL· GenBank· DDBJ | AAI15380.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133572 EMBL· GenBank· DDBJ | CAB63721.2 EMBL· GenBank· DDBJ | mRNA | ||
AB031230 EMBL· GenBank· DDBJ | BAA97672.1 EMBL· GenBank· DDBJ | mRNA |