Q9Y3S1 · WNK2_HUMAN
- ProteinSerine/threonine-protein kinase WNK2
- GeneWNK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The WNK2-SPAK/OSR1 kinase cascade is composed of WNK2, which mediates phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (By similarity).
Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters, regulating their activity (By similarity).
Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively (PubMed:21733846).
Activates SLC12A2, SCNN1A, SCNN1B, SCNN1D and SGK1 and inhibits SLC12A5 (PubMed:21733846).
Negatively regulates the EGF-induced activation of the ERK/MAPK-pathway and the downstream cell cycle progression (PubMed:17667937, PubMed:18593598).
Affects MAPK3/MAPK1 activity by modulating the activity of MAP2K1 and this modulation depends on phosphorylation of MAP2K1 by PAK1 (PubMed:17667937, PubMed:18593598).
WNK2 acts by interfering with the activity of PAK1 by controlling the balance of the activity of upstream regulators of PAK1 activity, RHOA and RAC1, which display reciprocal activity (PubMed:17667937, PubMed:18593598).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | intracellular signal transduction | |
Biological Process | monoatomic ion homeostasis | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | negative regulation of ERK1 and ERK2 cascade | |
Biological Process | positive regulation of canonical Wnt signaling pathway | |
Biological Process | positive regulation of sodium ion transmembrane transporter activity | |
Biological Process | protein autophosphorylation | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase WNK2
- 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 accessionQ9Y3S1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057114 | 828 | in dbSNP:rs10761203 | |||
Sequence: V → M | ||||||
Natural variant | VAR_059773 | 974 | in dbSNP:rs10114908 | |||
Sequence: R → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,635 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086822 | 1-2297 | UniProt | Serine/threonine-protein kinase WNK2 | |||
Sequence: MDGDGGRRDVPGTLMEPGRGAGPAGMAEPRAKAARPGPQRFLRRSVVESDQEEPPGLEAAEAPGPQPPQPLQRRVLLLCKTRRLIAERARGRPAAPAPAALVAQPGAPGAPADAGPEPVGTQEPGPDPIAAAVETAPAPDGGPREEAAATVRKEDEGAAEAKPEPGRTRRDEPEEEEDDEDDLKAVATSLDGRFLKFDIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKLERQRFKEEAEMLKGLQHPNIVRFYDFWESSAKGKRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVHDPEIKEIIGECICKNKEERYEIKDLLSHAFFAEDTGVRVELAEEDHGRKSTIALRLWVEDPKKLKGKPKDNGAIEFTFDLEKETPDEVAQEMIESGFFHESDVKIVAKSIRDRVALIQWRRERIWPALQPKEQQDVGSPDKARGPPVPLQVQVTYHAQAGQPGPPEPEEPEADQHLLPPTLPTSATSLASDSTFDSGQGSTVYSDSQSSQQSVMLGSLADAAPSPAQCVCSPPVSEGPVLPQSLPSLGAYQQPTAAPGLPVGSVPAPACPPSLQQHFPDPAMSFAPVLPPPSTPMPTGPGQPAPPGQQPPPLAQPTPLPQVLAPQPVVPLQPVPPHLPPYLAPASQVGAPAQLKPLQMPQAPLQPLAQVPPQMPPIPVVPPITPLAGIDGLPPALPDLPTATVPPVPPPQYFSPAVILPSLAAPLPPASPALPLQAVKLPHPPGAPLAMPCRTIVPNAPATIPLLAVAPPGVAALSIHSAVAQLPGQPVYPAAFPQMAPTDVPPSPHHTVQNMRATPPQPALPPQPTLPPQPVLPPQPTLPPQPVLPPQPTRPPQPVLPPQPMLPPQPVLPPQPALPVRPEPLQPHLPEQAAPAATPGSQILLGHPAPYAVDVAAQVPTVPVPPAAVLSPPLPEVLLPAAPELLPQFPSSLATVSASVQSVPTQTATLLPPANPPLPGGPGIASPCPTVQLTVEPVQEEQASQDKPPGLPQSCESYGGSDVTSGKELSDSCEGAFGGGRLEGRAARKHHRRSTRARSRQERASRPRLTILNVCNTGDKMVECQLETHNHKMVTFKFDLDGDAPDEIATYMVEHDFILQAERETFIEQMKDVMDKAEDMLSEDTDADRGSDPGTSPPHLSTCGLGTGEESRQSQANAPVYQQNVLHTGKRWFIICPVAEHPAPEAPESSPPLPLSSLPPEASQGPCRGLTLPCLPWRRAACGAVFLSLFSAESAQSKQPPDSAPYKDQLSSKEQPSFLASQQLLSQAGPSNPPGAPPAPLAPSSPPVTALPQDGAAPATSTMPEPASGTASQAGGPGTPQGLTSELETSQPLAETHEAPLAVQPLVVGLAPCTPAPEAASTRDASAPREPLPPPAPEPSPHSGTPQPALGQPAPLLPAAVGAVSLATSQLPSPPLGPTVPPQPPSALESDGEGPPPRVGFVDSTIKSLDEKLRTLLYQEHVPTSSASAGTPVEVGDRDFTLEPLRGDQPRSEVCGGDLALPPVPKEAVSGRVQLPQPLVEKSELAPTRGAVMEQGTSSSMTAESSPRSMLGYDRDGRQVASDSHVVPSVPQDVPAFVRPARVEPTDRDGGEAGESSAEPPPSDMGTVGGQASHPQTLGARALGSPRKRPEQQDVSSPAKTVGRFSVVSTQDEWTLASPHSLRYSAPPDVYLDEAPSSPDVKLAVRRAQTASSIEVGVGEPVSSDSGDEGPRARPPVQKQASLPVSGSVAGDFVKKATAFLQRPSRAGSLGPETPSRVGMKVPTISVTSFHSQSSYISSDNDSELEDADIKKELQSLREKHLKEISELQSQQKQEIEALYRRLGKPLPPNVGFFHTAPPTGRRRKTSKSKLKAGKLLNPLVRQLKVVASSTGHLADSSRGPPAKDPAQASVGLTADSTGLSGKAVQTQQPCSVRASLSSDICSGLASDGGGARGQGWTVYHPTSERVTYKSSSKPRARFLSGPVSVSIWSALKRLCLGKEHSSRSSTSSLAPGPEPGPQPALHVQAQVNNSNNKKGTFTDDLHKLVDEWTSKTVGAAQLKPTLNQLKQTQKLQDMEAQAGWAAPGEARAMTAPRAGVGMPRLPPAPGPLSTTVIPGAAPTLSVPTPDGALGTARRNQVWFGLRVPPTACCGHSTQPRGGQRVGSKTASFAASDPVRS | |||||||
Modified residue | 19 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 30 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 45 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 352 | UniProt | Phosphoserine; by autocatalysis | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 356 | UniProt | Phosphoserine; by autocatalysis | ||||
Sequence: S | |||||||
Modified residue | 560 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1150 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1262 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1262 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1588 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1611 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1685 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1736 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1777 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1798 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1805 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1817 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1817 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1818 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1818 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1843 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1844 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1846 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1862 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1862 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1889 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1889 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2067 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2067 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2157 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Autophosphorylation at Ser-352 and Ser-356 promotes its activity (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y3S1 | OXSR1 O95747 | 2 | EBI-948521, EBI-620853 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-75 | Disordered | ||||
Sequence: MDGDGGRRDVPGTLMEPGRGAGPAGMAEPRAKAARPGPQRFLRRSVVESDQEEPPGLEAAEAPGPQPPQPLQRRV | ||||||
Region | 89-183 | Disordered | ||||
Sequence: ARGRPAAPAPAALVAQPGAPGAPADAGPEPVGTQEPGPDPIAAAVETAPAPDGGPREEAAATVRKEDEGAAEAKPEPGRTRRDEPEEEEDDEDDL | ||||||
Compositional bias | 146-172 | Basic and acidic residues | ||||
Sequence: EAAATVRKEDEGAAEAKPEPGRTRRDE | ||||||
Domain | 195-453 | Protein kinase | ||||
Sequence: LKFDIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKLERQRFKEEAEMLKGLQHPNIVRFYDFWESSAKGKRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVHDPEIKEIIGECICKNKEERYEIKDLLSHAFF | ||||||
Region | 579-630 | Disordered | ||||
Sequence: AQAGQPGPPEPEEPEADQHLLPPTLPTSATSLASDSTFDSGQGSTVYSDSQS | ||||||
Compositional bias | 601-630 | Polar residues | ||||
Sequence: PTLPTSATSLASDSTFDSGQGSTVYSDSQS | ||||||
Region | 699-751 | Disordered | ||||
Sequence: FPDPAMSFAPVLPPPSTPMPTGPGQPAPPGQQPPPLAQPTPLPQVLAPQPVVP | ||||||
Compositional bias | 705-751 | Pro residues | ||||
Sequence: SFAPVLPPPSTPMPTGPGQPAPPGQQPPPLAQPTPLPQVLAPQPVVP | ||||||
Region | 917-1022 | Disordered | ||||
Sequence: PQMAPTDVPPSPHHTVQNMRATPPQPALPPQPTLPPQPVLPPQPTLPPQPVLPPQPTRPPQPVLPPQPMLPPQPVLPPQPALPVRPEPLQPHLPEQAAPAATPGSQ | ||||||
Compositional bias | 939-1009 | Pro residues | ||||
Sequence: PPQPALPPQPTLPPQPVLPPQPTLPPQPVLPPQPTRPPQPVLPPQPMLPPQPVLPPQPALPVRPEPLQPHL | ||||||
Compositional bias | 1117-1148 | Polar residues | ||||
Sequence: PVQEEQASQDKPPGLPQSCESYGGSDVTSGKE | ||||||
Region | 1117-1185 | Disordered | ||||
Sequence: PVQEEQASQDKPPGLPQSCESYGGSDVTSGKELSDSCEGAFGGGRLEGRAARKHHRRSTRARSRQERAS | ||||||
Compositional bias | 1165-1179 | Basic residues | ||||
Sequence: RAARKHHRRSTRARS | ||||||
Region | 1262-1297 | Disordered | ||||
Sequence: SEDTDADRGSDPGTSPPHLSTCGLGTGEESRQSQAN | ||||||
Compositional bias | 1275-1297 | Polar residues | ||||
Sequence: TSPPHLSTCGLGTGEESRQSQAN | ||||||
Region | 1323-1345 | Disordered | ||||
Sequence: APEAPESSPPLPLSSLPPEASQG | ||||||
Compositional bias | 1324-1339 | Pro residues | ||||
Sequence: PEAPESSPPLPLSSLP | ||||||
Compositional bias | 1374-1410 | Polar residues | ||||
Sequence: SAQSKQPPDSAPYKDQLSSKEQPSFLASQQLLSQAGP | ||||||
Region | 1374-1480 | Disordered | ||||
Sequence: SAQSKQPPDSAPYKDQLSSKEQPSFLASQQLLSQAGPSNPPGAPPAPLAPSSPPVTALPQDGAAPATSTMPEPASGTASQAGGPGTPQGLTSELETSQPLAETHEAP | ||||||
Compositional bias | 1411-1427 | Pro residues | ||||
Sequence: SNPPGAPPAPLAPSSPP | ||||||
Compositional bias | 1443-1472 | Polar residues | ||||
Sequence: MPEPASGTASQAGGPGTPQGLTSELETSQP | ||||||
Region | 1492-1586 | Disordered | ||||
Sequence: PCTPAPEAASTRDASAPREPLPPPAPEPSPHSGTPQPALGQPAPLLPAAVGAVSLATSQLPSPPLGPTVPPQPPSALESDGEGPPPRVGFVDSTI | ||||||
Compositional bias | 1508-1533 | Pro residues | ||||
Sequence: PREPLPPPAPEPSPHSGTPQPALGQP | ||||||
Compositional bias | 1554-1571 | Pro residues | ||||
Sequence: PPLGPTVPPQPPSALESD | ||||||
Region | 1621-1865 | Disordered | ||||
Sequence: TLEPLRGDQPRSEVCGGDLALPPVPKEAVSGRVQLPQPLVEKSELAPTRGAVMEQGTSSSMTAESSPRSMLGYDRDGRQVASDSHVVPSVPQDVPAFVRPARVEPTDRDGGEAGESSAEPPPSDMGTVGGQASHPQTLGARALGSPRKRPEQQDVSSPAKTVGRFSVVSTQDEWTLASPHSLRYSAPPDVYLDEAPSSPDVKLAVRRAQTASSIEVGVGEPVSSDSGDEGPRARPPVQKQASLPV | ||||||
Compositional bias | 1672-1687 | Polar residues | ||||
Sequence: VMEQGTSSSMTAESSP | ||||||
Compositional bias | 1770-1798 | Polar residues | ||||
Sequence: PEQQDVSSPAKTVGRFSVVSTQDEWTLAS | ||||||
Region | 1970-1990 | Disordered | ||||
Sequence: NVGFFHTAPPTGRRRKTSKSK | ||||||
Region | 2011-2031 | Disordered | ||||
Sequence: TGHLADSSRGPPAKDPAQASV | ||||||
Region | 2123-2142 | Disordered | ||||
Sequence: SRSSTSSLAPGPEPGPQPAL | ||||||
Region | 2269-2297 | Disordered | ||||
Sequence: CCGHSTQPRGGQRVGSKTASFAASDPVRS | ||||||
Compositional bias | 2273-2291 | Polar residues | ||||
Sequence: STQPRGGQRVGSKTASFAA |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q9Y3S1-1
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
- Length2,297
- Mass (Da)242,676
- Last updated2004-02-02 v4
- Checksum33D2EF2BFA6A1BD2
Q9Y3S1-2
- Name2
- Differences from canonical
- 1345-1381: Missing
- 2247-2261: DGALGTARRNQVWFG → GSCGPRAVSTPTSYT
- 2262-2297: Missing
Q9Y3S1-3
- Name3
- NoteIncomplete sequence.
Q9Y3S1-4
- Name4
- Differences from canonical
- 2248-2254: GALGTAR → PESEKPD
- 2255-2297: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_050639 | 1-14 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 146-172 | Basic and acidic residues | ||||
Sequence: EAAATVRKEDEGAAEAKPEPGRTRRDE | ||||||
Compositional bias | 601-630 | Polar residues | ||||
Sequence: PTLPTSATSLASDSTFDSGQGSTVYSDSQS | ||||||
Alternative sequence | VSP_050640 | 680-731 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 705-751 | Pro residues | ||||
Sequence: SFAPVLPPPSTPMPTGPGQPAPPGQQPPPLAQPTPLPQVLAPQPVVP | ||||||
Alternative sequence | VSP_050641 | 843-845 | in isoform 3 | |||
Sequence: LAA → RTR | ||||||
Alternative sequence | VSP_050642 | 846-2297 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 939-1009 | Pro residues | ||||
Sequence: PPQPALPPQPTLPPQPVLPPQPTLPPQPVLPPQPTRPPQPVLPPQPMLPPQPVLPPQPALPVRPEPLQPHL | ||||||
Compositional bias | 1117-1148 | Polar residues | ||||
Sequence: PVQEEQASQDKPPGLPQSCESYGGSDVTSGKE | ||||||
Compositional bias | 1165-1179 | Basic residues | ||||
Sequence: RAARKHHRRSTRARS | ||||||
Compositional bias | 1275-1297 | Polar residues | ||||
Sequence: TSPPHLSTCGLGTGEESRQSQAN | ||||||
Compositional bias | 1324-1339 | Pro residues | ||||
Sequence: PEAPESSPPLPLSSLP | ||||||
Alternative sequence | VSP_050643 | 1345-1381 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1374-1410 | Polar residues | ||||
Sequence: SAQSKQPPDSAPYKDQLSSKEQPSFLASQQLLSQAGP | ||||||
Compositional bias | 1411-1427 | Pro residues | ||||
Sequence: SNPPGAPPAPLAPSSPP | ||||||
Compositional bias | 1443-1472 | Polar residues | ||||
Sequence: MPEPASGTASQAGGPGTPQGLTSELETSQP | ||||||
Compositional bias | 1508-1533 | Pro residues | ||||
Sequence: PREPLPPPAPEPSPHSGTPQPALGQP | ||||||
Compositional bias | 1554-1571 | Pro residues | ||||
Sequence: PPLGPTVPPQPPSALESD | ||||||
Compositional bias | 1672-1687 | Polar residues | ||||
Sequence: VMEQGTSSSMTAESSP | ||||||
Compositional bias | 1770-1798 | Polar residues | ||||
Sequence: PEQQDVSSPAKTVGRFSVVSTQDEWTLAS | ||||||
Alternative sequence | VSP_050644 | 2247-2261 | in isoform 2 | |||
Sequence: DGALGTARRNQVWFG → GSCGPRAVSTPTSYT | ||||||
Alternative sequence | VSP_050645 | 2248-2254 | in isoform 4 | |||
Sequence: GALGTAR → PESEKPD | ||||||
Alternative sequence | VSP_050646 | 2255-2297 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_050647 | 2262-2297 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 2273-2291 | Polar residues | ||||
Sequence: STQPRGGQRVGSKTASFAA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ242724 EMBL· GenBank· DDBJ | CAB44308.5 EMBL· GenBank· DDBJ | mRNA | ||
AL354991 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL390760 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL583839 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AB044546 EMBL· GenBank· DDBJ | BAB18648.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051547 EMBL· GenBank· DDBJ | BAB21851.2 EMBL· GenBank· DDBJ | mRNA | ||
BC037965 EMBL· GenBank· DDBJ | AAH37965.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |