Q05397 · FAK1_HUMAN
- ProteinFocal adhesion kinase 1
- GenePTK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1052 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.
Isoform 6
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Activity regulation
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFocal adhesion kinase 1
- EC number
- Short namesFADK 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ05397
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_041682 | 292 | ||||
Sequence: H → P | ||||||
Natural variant | VAR_041683 | 292 | ||||
Sequence: H → Q | ||||||
Mutagenesis | 397 | Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. Reduces phosphorylation of NEDD9. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_041684 | 793 | in a glioblastoma multiforme sample; somatic mutation | |||
Sequence: V → A | ||||||
Mutagenesis | 928 | Loss of interaction with TGFB1I1. | ||||
Sequence: V → G | ||||||
Natural variant | VAR_041685 | 1030 | ||||
Sequence: D → E | ||||||
Mutagenesis | 1034 | Loss of interaction with TGFB1I1. | ||||
Sequence: L → S | ||||||
Natural variant | VAR_041686 | 1044 | in a metastatic melanoma sample; somatic mutation | |||
Sequence: K → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,077 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 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-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000088077 | 2-1052 | UniProt | Focal adhesion kinase 1 | |||
Sequence: AAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH | |||||||
Modified residue | 5 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 13 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 16 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 29 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 152 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 406 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 407 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 441 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 570 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 570 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 575 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 576 | UniProt | Phosphotyrosine; by RET and SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 577 | UniProt | Phosphotyrosine; by RET and SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 580 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 705 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 708 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 716 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 722 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 722 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 732 | UniProt | Phosphoserine; by CDK5 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 840 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 843 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 843 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 850 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 861 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 861 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 887 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 890 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 892 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 893 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 898 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 910 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 910 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 914 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 914 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 925 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 925 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Developmental stage
Isoform 6
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL (PubMed:29069646).
Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 (By similarity).
Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2. Interacts with CD36. Interacts with EMP2; regulates PTK2 activation and localization (PubMed:19494199).
Interacts with DSCAM (By similarity).
Interacts with AMBRA1 (By similarity).
Interacts (when tyrosine-phosphorylated) with tensin TNS1; the interaction is increased by phosphorylation of TNS1 (PubMed:20798394).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-27 | Disordered | ||||
Sequence: MAAAYLDPNLNHTPNSSTKTHLGTGME | ||||||
Compositional bias | 9-24 | Polar residues | ||||
Sequence: NLNHTPNSSTKTHLGT | ||||||
Domain | 35-355 | FERM | ||||
Sequence: RVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTS | ||||||
Domain | 422-680 | Protein kinase | ||||
Sequence: IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL | ||||||
Region | 684-734 | Disordered | ||||
Sequence: KAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQ | ||||||
Region | 707-1052 | Interaction with TGFB1I1 | ||||
Sequence: GSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH | ||||||
Region | 839-922 | Disordered | ||||
Sequence: LSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSND | ||||||
Compositional bias | 866-880 | Pro residues | ||||
Sequence: KPDPAAPPKKPPRPG | ||||||
Compositional bias | 890-922 | Polar residues | ||||
Sequence: SLSSPADSYNEGVKLQPQEISPPPTANLDRSND | ||||||
Region | 912-1052 | Interaction with ARHGEF28 | ||||
Sequence: PPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative promoter usage & Alternative splicing.
Q05397-1
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
- Length1,052
- Mass (Da)119,233
- Last updated1998-07-15 v2
- ChecksumD8A4C15138AB0243
Q05397-2
- Name2
Q05397-3
- Name3
Q05397-4
- Name4
Q05397-5
- Name5
Q05397-6
- Name6
- SynonymsFRNK
- NoteProduced by alternative promoter usage.
- Differences from canonical
- 1-692: Missing
Q05397-7
- Name7
- Differences from canonical
- 744-789: Missing
Computationally mapped potential isoform sequences
There are 33 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7ESA6 | E7ESA6_HUMAN | PTK2 | 1096 | ||
B4DWJ1 | B4DWJ1_HUMAN | PTK2 | 362 | ||
H0YBZ1 | H0YBZ1_HUMAN | PTK2 | 753 | ||
H0YAS0 | H0YAS0_HUMAN | PTK2 | 72 | ||
H0YB99 | H0YB99_HUMAN | PTK2 | 319 | ||
H0YB33 | H0YB33_HUMAN | PTK2 | 128 | ||
H0YBP1 | H0YBP1_HUMAN | PTK2 | 1017 | ||
H0YB16 | H0YB16_HUMAN | PTK2 | 724 | ||
E9PEI4 | E9PEI4_HUMAN | PTK2 | 680 | ||
A0A8Q3WLM4 | A0A8Q3WLM4_HUMAN | PTK2 | 1096 | ||
A0A1D5RMT1 | A0A1D5RMT1_HUMAN | PTK2 | 8 | ||
E5RIK4 | E5RIK4_HUMAN | PTK2 | 65 | ||
E5RII9 | E5RII9_HUMAN | PTK2 | 67 | ||
E5RIR5 | E5RIR5_HUMAN | PTK2 | 72 | ||
E5RJI4 | E5RJI4_HUMAN | PTK2 | 168 | ||
E5RJQ2 | E5RJQ2_HUMAN | PTK2 | 132 | ||
E5RJP0 | E5RJP0_HUMAN | PTK2 | 122 | ||
E5RJN1 | E5RJN1_HUMAN | PTK2 | 14 | ||
E5RFW9 | E5RFW9_HUMAN | PTK2 | 121 | ||
E5RG86 | E5RG86_HUMAN | PTK2 | 59 | ||
E5RG66 | E5RG66_HUMAN | PTK2 | 119 | ||
E5RG80 | E5RG80_HUMAN | PTK2 | 133 | ||
E5RG54 | E5RG54_HUMAN | PTK2 | 66 | ||
E5RGA6 | E5RGA6_HUMAN | PTK2 | 156 | ||
E5RH48 | E5RH48_HUMAN | PTK2 | 107 | ||
E5RGP1 | E5RGP1_HUMAN | PTK2 | 79 | ||
E5RH01 | E5RH01_HUMAN | PTK2 | 117 | ||
E5RH08 | E5RH08_HUMAN | PTK2 | 51 | ||
E5RHD8 | E5RHD8_HUMAN | PTK2 | 115 | ||
E5RHK7 | E5RHK7_HUMAN | PTK2 | 67 | ||
E5RI29 | E5RI29_HUMAN | PTK2 | 124 | ||
E5RI72 | E5RI72_HUMAN | PTK2 | 120 | ||
E5RI03 | E5RI03_HUMAN | PTK2 | 120 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_004967 | 1-181 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_042168 | 1-692 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 9-24 | Polar residues | ||||
Sequence: NLNHTPNSSTKTHLGT | ||||||
Alternative sequence | VSP_004968 | 182-189 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: EMRGNALE → MSDYWVVG | ||||||
Sequence conflict | 184 | in Ref. 3; BAG65198 | ||||
Sequence: R → L | ||||||
Sequence conflict | 211 | in Ref. 3; BAG65198 | ||||
Sequence: L → I | ||||||
Alternative sequence | VSP_004969 | 472 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE | ||||||
Alternative sequence | VSP_004971 | 579-583 | in isoform 4 | |||
Sequence: ASKGK → GKKSG | ||||||
Alternative sequence | VSP_004972 | 584-1052 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004973 | 677-706 | in isoform 3 | |||
Sequence: STILEEEKAQQEERMRMESRRQATVSWDSG → FQNPAQMLPASGRLPNQPCPERENYSFATF | ||||||
Alternative sequence | VSP_004974 | 707-1052 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_057268 | 744-789 | in isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 778 | in Ref. 2; AAA35819 | ||||
Sequence: P → S | ||||||
Alternative sequence | VSP_004970 | 834-854 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 866-880 | Pro residues | ||||
Sequence: KPDPAAPPKKPPRPG | ||||||
Alternative sequence | VSP_042169 | 868 | in isoform 5 | |||
Sequence: D → GKEEKNWAERN | ||||||
Compositional bias | 890-922 | Polar residues | ||||
Sequence: SLSSPADSYNEGVKLQPQEISPPPTANLDRSND | ||||||
Alternative sequence | VSP_042170 | 903 | in isoform 5 | |||
Sequence: K → KPWR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L13616 EMBL· GenBank· DDBJ | AAA58469.1 EMBL· GenBank· DDBJ | mRNA | ||
L05186 EMBL· GenBank· DDBJ | AAA35819.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304356 EMBL· GenBank· DDBJ | BAG65198.1 EMBL· GenBank· DDBJ | mRNA | ||
AC067931 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC100860 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC105009 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC105235 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF458878 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF458882 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC035404 EMBL· GenBank· DDBJ | AAH35404.1 EMBL· GenBank· DDBJ | mRNA |