Q02297 · NRG1_HUMAN
- ProteinPro-neuregulin-1, membrane-bound isoform
- GeneNRG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids640 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to ERBB3 (PubMed:20682778).
Acts as a ligand for integrins and binds (via EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and ERRB3 are essential for NRG1-ERBB signaling. Induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:20682778).
Ligand-dependent ERBB4 endocytosis is essential for the NRG1-mediated activation of these kinases in neurons (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 34 | Breakpoint for translocation to form gamma-heregulin | ||||
Sequence: A |
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePro-neuregulin-1, membrane-bound isoform
- Short namesPro-NRG1
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ02297
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Pro-neuregulin-1, membrane-bound isoform
Neuregulin-1
Isoform 8
Isoform 9
Isoform 10
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-242 | Extracellular | ||||
Sequence: SGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKR | ||||||
Transmembrane | 243-265 | Helical; Note=Internal signal sequence | ||||
Sequence: VLTITGICIALLVVGIMCVVAYC | ||||||
Topological domain | 266-640 | Cytoplasmic | ||||
Sequence: KTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_009307 | 38 | in dbSNP:rs3924999 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_082866 | 46 | In isoform Q02297-10; in dbSNP:rs3735774 | |||
Sequence: G → R | ||||||
Natural variant | VAR_082867 | 127 | In isoform Q02297-10; in dbSNP:rs34822181 | |||
Sequence: A → P | ||||||
Mutagenesis | 181 | Defective in integrin-binding and in inducing ERBB3 phosphorylation; when associated with or without E-185 or E-187. No effect on ERBB3-binding, defective in integrin-binding and in ternary complex formation with ERBB3 and integrins, and defective in inducing NRG1-ERBB signaling; when associated with E-185 and E-187. | ||||
Sequence: K → E | ||||||
Mutagenesis | 185 | Defective in integrin-binding and in inducing ERBB3 phosphorylation; when associated with or without E-181 or E-187. No effect on ERBB3-binding, defective in integrin-binding and in ternary complex formation with ERBB3 and integrins, and defective in inducing NRG1-ERBB signaling; when associated with E-181 and E-187. | ||||
Sequence: K → E | ||||||
Mutagenesis | 187 | Defective in integrin-binding and in inducing ERBB3 phosphorylation; when associated with or without E-181 or E-185. No effect on ERBB3-binding, defective in integrin-binding and in ternary complex formation with ERBB3 and integrins, and defective in inducing NRG1-ERBB signaling; when associated with E-181 and E-185. | ||||
Sequence: K → E | ||||||
Natural variant | VAR_053531 | 289 | in dbSNP:rs10503929 | |||
Sequence: M → T | ||||||
Natural variant | VAR_009308 | 463 | ||||
Sequence: M → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 994 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for propeptide, chain, modified residue (large scale data), disulfide bond, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Propeptide | PRO_0000019462 | 1-19 | UniProt | ||||
Sequence: MSERKEGRGKGKGKKKERG | |||||||
Chain | PRO_0000019464 | 20-241 | UniProt | Neuregulin-1 | |||
Sequence: SGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQK | |||||||
Chain | PRO_0000019463 | 20-640 | UniProt | Pro-neuregulin-1, membrane-bound isoform | |||
Sequence: SGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 57↔112 | UniProt | |||||
Sequence: CETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMC | |||||||
Glycosylation | 120 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 126 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 164 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 182↔196 | UniProt | |||||
Sequence: CAEKEKTFCVNGGEC | |||||||
Disulfide bond | 190↔210 | UniProt | |||||
Sequence: CVNGGECFMVKDLSNPSRYLC | |||||||
Disulfide bond | 212↔221 | UniProt | |||||
Sequence: CQPGFTGARC | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 435 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms a ternary complex with ERBB3 and ITGAV:ITGB3 or ITGA6:ITGB4 (PubMed:20682778).
Interacts with NRDC and BACE1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q02297-10 | ASGR2 P07307-3 | 3 | EBI-12842334, EBI-12808270 | |
BINARY | Q02297-10 | CD72 P21854 | 3 | EBI-12842334, EBI-307924 | |
BINARY | Q02297-10 | JAGN1 Q8N5M9 | 3 | EBI-12842334, EBI-10266796 | |
BINARY | Q02297-10 | LAPTM4B Q86VI4 | 3 | EBI-12842334, EBI-3267258 | |
BINARY | Q02297-10 | MS4A4A Q96JQ5 | 3 | EBI-12842334, EBI-12820341 | |
BINARY | Q02297-10 | PLP1 P60201-2 | 3 | EBI-12842334, EBI-12188331 | |
BINARY | Q02297-10 | TMEM54 Q969K7 | 3 | EBI-12842334, EBI-3922833 | |
BINARY | Q02297-6 | ERBB3 P21860 | 2 | EBI-15651799, EBI-720706 | |
BINARY | Q02297-6 | ERBB4 Q15303 | 3 | EBI-15651799, EBI-80371 | |
BINARY | Q02297-7 | ERBB2 P04626 | 2 | EBI-2460927, EBI-641062 | |
BINARY | Q02297-7 | ERBB3 P21860 | 3 | EBI-2460927, EBI-720706 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-53 | Disordered | ||||
Sequence: MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKL | ||||||
Domain | 37-128 | Ig-like C2-type | ||||
Sequence: PRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANIT | ||||||
Domain | 178-222 | EGF-like | ||||
Sequence: HLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCT | ||||||
Region | 334-360 | Disordered | ||||
Sequence: TSHYTSTAHHSTTVTQTPSHSWSNGHT | ||||||
Compositional bias | 375-389 | Polar residues | ||||
Sequence: SVENSRHSSPTGGPR | ||||||
Region | 375-399 | Disordered | ||||
Sequence: SVENSRHSSPTGGPRGRLNGTGGPR | ||||||
Region | 433-461 | Disordered | ||||
Sequence: RMSPVDFHTPSSPKSPPSEMSPPVSSMTV | ||||||
Region | 524-588 | Disordered | ||||
Sequence: EYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPF | ||||||
Compositional bias | 559-573 | Polar residues | ||||
Sequence: RLEVDSNTSSQSSNS |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 11 isoforms produced by Alternative splicing. Additional isoforms seem to exist. Isoforms have been classified as type I NRGs (isoforms with an Ig domain and a glycosylation domain, isoforms 1-8), type II NRGs (isoforms with an Ig domain but no glycosylation domain, isoform 9), type III NRGs (isoforms with a Cys-rich domain, isoform 10) and type IV NRGs (isoforms with additional 5' exons, isoform 11). All these isoforms perform distinct tissue-specific functions.
Q02297-1
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
- SynonymsAlpha
- NotePotential internal signal sequence at positions 76-100.
- Length640
- Mass (Da)70,392
- Last updated2007-01-23 v3
- ChecksumC30D3F614AADFF62
Q02297-2
- Name2
- SynonymsAlpha1A
- Differences from canonical
- 234-234: K → KHLGIEFIE
Q02297-3
- Name3
- SynonymsAlpha2B
Q02297-4
- Name4
- SynonymsAlpha3
Q02297-6
- Name6
- SynonymsBeta1, Beta1A
- Differences from canonical
- 213-234: QPGFTGARCTENVPMKVQNQEK → PNEFTGDRCQNYVMASFYKHLGIEFME
Q02297-7
- Name7
- SynonymsBeta2
- Differences from canonical
- 213-233: QPGFTGARCTENVPMKVQNQE → PNEFTGDRCQNYVMASFY
Q02297-8
- Name8
- SynonymsBeta3, GGFHFB1
Q02297-9
- Name9
- SynonymsGGF2, GGFHPP2
- Differences from canonical
- 1-33: MSERKEGRGKGKGKKKERGSGKKPESAAGSQSP → MRWRRAPRRSGRPGPRAQRPGSAARSSPPLPLLPLLLLLGTAALAPGAAAGNEAAPAGASVCYSSPPSVGSVQELAQRAAVVIEGKVHPQRRQQGALDRKAAAAAGEAGAWGGDREPPAAGPRALGPPAEEPLLAANGTVPSWPTAPVPSAGEPGEEAPYLVKVHQVWAVKAGGLKKDSLLTVRLGTWGHPAFPSCGRLKEDSRYIFFMEPDANSTSRAPAAFRASFPPLETGRNLKKEVSRVLCKRC
- 134-168: EIITGMPASTEGAYVSSESPIRISVSTEGANTSSS → A
- 213-241: QPGFTGARCTENVPMKVQNQEKAEELYQK → PNEFTGDRCQNYVMASFYSTSTPFLSLPE
- 242-640: Missing
Q02297-10
- Name10
- SynonymsSMDF
- NotePotential internal signal sequence at positions 76-100.
- Differences from canonical
- 1-166: Missing
- 167-167: S → MEIYSPDMSEVAAERSSSPSTQLSADPSLDGLPAAEDMPEPQTEDGRTPGLVGLAVPCCACLEAERLRGCLNSEKICIVPILACLVSLCLCIAGLKWVFVDKIFEYDSPTHLDPGGLGQDPIISLDATAASAVWVSSEAYTSPVSRAQSESEVQVTVQGDKAVVSFEPSAAPTPKNRIFAFSFLPSTAPSFPSPTRNPEVRTPKSATQPQTTETNLQTAPKL
- 213-241: QPGFTGARCTENVPMKVQNQEKAEELYQK → PNEFTGDRCQNYVMASFYSTSTPFLSLPE
- 242-640: Missing
Q02297-11
- Name11
- SynonymsType IV-beta1a
Q02297-12
- Name12
Computationally mapped potential isoform sequences
There are 19 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YDC2 | H0YDC2_HUMAN | NRG1 | 236 | ||
H0YCP0 | H0YCP0_HUMAN | NRG1 | 126 | ||
H0YBA3 | H0YBA3_HUMAN | NRG1 | 713 | ||
A0A494BZT4 | A0A494BZT4_HUMAN | NRG1 | 214 | ||
A0A5F9ZHA5 | A0A5F9ZHA5_HUMAN | NRG1 | 168 | ||
A0A494C1G2 | A0A494C1G2_HUMAN | NRG1 | 387 | ||
A0A494C1F5 | A0A494C1F5_HUMAN | NRG1 | 624 | ||
A0A494C1F8 | A0A494C1F8_HUMAN | NRG1 | 607 | ||
A0A494C1B5 | A0A494C1B5_HUMAN | NRG1 | 483 | ||
A0A494C0L9 | A0A494C0L9_HUMAN | NRG1 | 522 | ||
A0A494C0K4 | A0A494C0K4_HUMAN | NRG1 | 459 | ||
A0A494C0Q4 | A0A494C0Q4_HUMAN | NRG1 | 700 | ||
A0A494C0T5 | A0A494C0T5_HUMAN | NRG1 | 130 | ||
A0A494C114 | A0A494C114_HUMAN | NRG1 | 207 | ||
A0A494C054 | A0A494C054_HUMAN | NRG1 | 155 | ||
A0A494C043 | A0A494C043_HUMAN | NRG1 | 461 | ||
E5RIG8 | E5RIG8_HUMAN | NRG1 | 135 | ||
E5RHQ1 | E5RHQ1_HUMAN | NRG1 | 101 | ||
E5RHP6 | E5RHP6_HUMAN | NRG1 | 308 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037563 | 1-21 | in isoform 11 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_003425 | 1-33 | in isoform 9 | |||
Sequence: MSERKEGRGKGKGKKKERGSGKKPESAAGSQSP → MRWRRAPRRSGRPGPRAQRPGSAARSSPPLPLLPLLLLLGTAALAPGAAAGNEAAPAGASVCYSSPPSVGSVQELAQRAAVVIEGKVHPQRRQQGALDRKAAAAAGEAGAWGGDREPPAAGPRALGPPAEEPLLAANGTVPSWPTAPVPSAGEPGEEAPYLVKVHQVWAVKAGGLKKDSLLTVRLGTWGHPAFPSCGRLKEDSRYIFFMEPDANSTSRAPAAFRASFPPLETGRNLKKEVSRVLCKRC | ||||||
Alternative sequence | VSP_037562 | 1-166 | in isoform 10 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_037564 | 22-33 | in isoform 11 | |||
Sequence: KKPESAAGSQSP → MGKGRAGRVGTT | ||||||
Sequence conflict | 94 | in Ref. 2; AAA19953 | ||||
Sequence: K → A | ||||||
Sequence conflict | 107 | in Ref. 10; ABQ53539 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_003426 | 134-168 | in isoform 9 and isoform 11 | |||
Sequence: EIITGMPASTEGAYVSSESPIRISVSTEGANTSSS → A | ||||||
Alternative sequence | VSP_037565 | 167 | in isoform 10 | |||
Sequence: S → MEIYSPDMSEVAAERSSSPSTQLSADPSLDGLPAAEDMPEPQTEDGRTPGLVGLAVPCCACLEAERLRGCLNSEKICIVPILACLVSLCLCIAGLKWVFVDKIFEYDSPTHLDPGGLGQDPIISLDATAASAVWVSSEAYTSPVSRAQSESEVQVTVQGDKAVVSFEPSAAPTPKNRIFAFSFLPSTAPSFPSPTRNPEVRTPKSATQPQTTETNLQTAPKL | ||||||
Alternative sequence | VSP_003427 | 213-233 | in isoform 7 and isoform 12 | |||
Sequence: QPGFTGARCTENVPMKVQNQE → PNEFTGDRCQNYVMASFY | ||||||
Alternative sequence | VSP_003428 | 213-234 | in isoform 6 and isoform 11 | |||
Sequence: QPGFTGARCTENVPMKVQNQEK → PNEFTGDRCQNYVMASFYKHLGIEFME | ||||||
Alternative sequence | VSP_003429 | 213-241 | in isoform 8, isoform 9 and isoform 10 | |||
Sequence: QPGFTGARCTENVPMKVQNQEKAEELYQK → PNEFTGDRCQNYVMASFYSTSTPFLSLPE | ||||||
Alternative sequence | VSP_003431 | 234 | in isoform 2 | |||
Sequence: K → KHLGIEFIE | ||||||
Alternative sequence | VSP_003432 | 234-247 | in isoform 4 | |||
Sequence: KAEELYQKRVLTIT → SAQMSLLVIAAKTT | ||||||
Alternative sequence | VSP_003430 | 242-640 | in isoform 8, isoform 9 and isoform 10 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_003433 | 248-640 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 261 | in Ref. 10; ABQ53540 | ||||
Sequence: V → L | ||||||
Compositional bias | 375-389 | Polar residues | ||||
Sequence: SVENSRHSSPTGGPR | ||||||
Sequence conflict | 414 | in Ref. 2; AAA19953 | ||||
Sequence: S → F | ||||||
Alternative sequence | VSP_003434 | 424-462 | in isoform 3 | |||
Sequence: YVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVS → HNLIAELRRNKAHRSKCMQIQLSATHLRSSSIPHLGFIL | ||||||
Alternative sequence | VSP_046417 | 424-640 | in isoform 12 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_003435 | 463-640 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 535 | in Ref. 2; AAA19951 | ||||
Sequence: Q → R | ||||||
Compositional bias | 559-573 | Polar residues | ||||
Sequence: RLEVDSNTSSQSSNS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M94165 EMBL· GenBank· DDBJ | AAA58638.1 EMBL· GenBank· DDBJ | mRNA | ||
M94166 EMBL· GenBank· DDBJ | AAA58639.1 EMBL· GenBank· DDBJ | mRNA | ||
M94167 EMBL· GenBank· DDBJ | AAA58640.1 EMBL· GenBank· DDBJ | mRNA | ||
M94168 EMBL· GenBank· DDBJ | AAA58641.1 EMBL· GenBank· DDBJ | mRNA | ||
U02325 EMBL· GenBank· DDBJ | AAA19950.1 EMBL· GenBank· DDBJ | mRNA | ||
U02326 EMBL· GenBank· DDBJ | AAA19951.1 EMBL· GenBank· DDBJ | mRNA | ||
U02327 EMBL· GenBank· DDBJ | AAA19952.1 EMBL· GenBank· DDBJ | mRNA | ||
U02328 EMBL· GenBank· DDBJ | AAA19953.1 EMBL· GenBank· DDBJ | mRNA | ||
U02329 EMBL· GenBank· DDBJ | AAA19954.1 EMBL· GenBank· DDBJ | mRNA | ||
U02330 EMBL· GenBank· DDBJ | AAA19955.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
L12260 EMBL· GenBank· DDBJ | AAB59622.1 EMBL· GenBank· DDBJ | mRNA | ||
L12261 EMBL· GenBank· DDBJ | AAB59358.1 EMBL· GenBank· DDBJ | mRNA | ||
L41827 EMBL· GenBank· DDBJ | AAC41764.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289927 EMBL· GenBank· DDBJ | BAF82616.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298132 EMBL· GenBank· DDBJ | BAH12729.1 EMBL· GenBank· DDBJ | mRNA | ||
AC021909 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022833 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022850 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC023948 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC068359 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC068931 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC083977 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC103675 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104000 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104029 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC113209 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF009227 EMBL· GenBank· DDBJ | AAC51756.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF491780 EMBL· GenBank· DDBJ | AAM71137.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF491780 EMBL· GenBank· DDBJ | AAM71139.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF491780 EMBL· GenBank· DDBJ | AAM71140.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF372273 EMBL· GenBank· DDBJ | ABQ53539.1 EMBL· GenBank· DDBJ | mRNA | ||
EF372274 EMBL· GenBank· DDBJ | ABQ53540.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471080 EMBL· GenBank· DDBJ | EAW63411.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC064587 EMBL· GenBank· DDBJ | AAH64587.1 EMBL· GenBank· DDBJ | mRNA | ||
BC073871 EMBL· GenBank· DDBJ | AAH73871.1 EMBL· GenBank· DDBJ | mRNA | ||
AF026146 EMBL· GenBank· DDBJ | AAD01795.1 EMBL· GenBank· DDBJ | mRNA | ||
BK000383 EMBL· GenBank· DDBJ | DAA00044.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK000383 EMBL· GenBank· DDBJ | DAA00045.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK000383 EMBL· GenBank· DDBJ | DAA00046.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK000383 EMBL· GenBank· DDBJ | DAA00047.1 EMBL· GenBank· DDBJ | Genomic DNA |