Q0IHQ8 · STK10_XENTR
- ProteinSerine/threonine-protein kinase 10
- Genestk10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids951 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
May act as a polo kinase kinase by mediating phosphorylation of plk1/plx1 and subsequent activation of plk1/plx1 during oocyte maturation.
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | protein autophosphorylation | |
Biological Process | regulation of lymphocyte migration |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase 10
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Silurana
Accessions
- Primary accessionQ0IHQ8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000414715 | 1-951 | Serine/threonine-protein kinase 10 | |||
Sequence: MAFANFRRILRLPNFEKKRLREYEHVRRDLDPNQVWEIIGELGDGAFGKVYKAKNKETGILAAAKVIETKNEEELEDYMVEIEILATCNHHFIVKLLGSYYWEGKLWIMIEFCPGGAVDAIMLELDRGLKEPEIRTICRQMLEGLTYLHSMKMIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSSPSKWSPEFHNFLKTALDKNPETRPSAAQLLEHPFVKKVSGNKPLRDLVAEAKAEVLDEIEENGEVEEEEASDTPSSNKSVSQSALGEKDKHTGKEHVGNGIKAEPQNTDSQADIHSQKRNHEGKNYPEHNRHDAVNGKPDIIILNPVSSNHEPKRNSAAESYRNEEHGSAVSSNQRPKSSQSDRQSVELVPNGSFDSPTRYFTGWSKRDSDSGSNSASESMDISMNLSADLSINKETGSLSLRESRLHKKTLKRTRRFVVDGVEVSITTSKIIGDDEKKDEEMRFLRRQELRELRLLQKEEHRNQAQLTSKHSFQMEQMLRRFEQEMNSKRKFYDSELEALERHQKQQIERMEQEHALRRRDEARRIRTEQERDHVKFLEQLKLRKKELKAQVEKLPRQQRRDAMKVQMDDFAQKKHIEEQQFLNKQKEDLTLALRVIVLENRKEIYNKEREFLNKKQQLLRDREAVIWDLEERHLQERHQLVKQQLKDQYFLQRHELLRKHEKEQEQMQRYNQRMMEQLKLRQQQERARLPKNQKAEAKTRMTMFKKSLHISPSGSAAEQREKIKQFSLQEEKRQKAERLQQQQKHEHQLLEMQAECDCNVRDLLQMQNEKCHLLVEHETQKLKTLDEHHIQMIREWRENLRPRKKALEDELEHKKEEQEMFFRMNEEVAGHPFPSNKPAKFYSFSSPEAS | ||||||
Modified residue | 483 | Phosphoserine; by PLK1 | ||||
Sequence: S | ||||||
Modified residue | 487 | Phosphoserine; by PLK1 | ||||
Sequence: S | ||||||
Modified residue | 491 | Phosphoserine; by PLK1 | ||||
Sequence: S |
Post-translational modification
Autophosphorylates. Phosphorylated by plk1/plx1, suggesting the existence of a feedback loop with plk1/plx1. activation of the protein (By similarity).
Keywords
- PTM
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-294 | Protein kinase | ||||
Sequence: WEIIGELGDGAFGKVYKAKNKETGILAAAKVIETKNEEELEDYMVEIEILATCNHHFIVKLLGSYYWEGKLWIMIEFCPGGAVDAIMLELDRGLKEPEIRTICRQMLEGLTYLHSMKMIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSSPSKWSPEFHNFLKTALDKNPETRPSAAQLLEHPFV | ||||||
Region | 319-479 | Disordered | ||||
Sequence: EENGEVEEEEASDTPSSNKSVSQSALGEKDKHTGKEHVGNGIKAEPQNTDSQADIHSQKRNHEGKNYPEHNRHDAVNGKPDIIILNPVSSNHEPKRNSAAESYRNEEHGSAVSSNQRPKSSQSDRQSVELVPNGSFDSPTRYFTGWSKRDSDSGSNSASES | ||||||
Compositional bias | 343-357 | Basic and acidic residues | ||||
Sequence: ALGEKDKHTGKEHVG | ||||||
Compositional bias | 373-395 | Basic and acidic residues | ||||
Sequence: IHSQKRNHEGKNYPEHNRHDAVN | ||||||
Compositional bias | 425-479 | Polar residues | ||||
Sequence: EHGSAVSSNQRPKSSQSDRQSVELVPNGSFDSPTRYFTGWSKRDSDSGSNSASES | ||||||
Coiled coil | 583-723 | |||||
Sequence: EQEMNSKRKFYDSELEALERHQKQQIERMEQEHALRRRDEARRIRTEQERDHVKFLEQLKLRKKELKAQVEKLPRQQRRDAMKVQMDDFAQKKHIEEQQFLNKQKEDLTLALRVIVLENRKEIYNKEREFLNKKQQLLRDR | ||||||
Region | 785-804 | Disordered | ||||
Sequence: QERARLPKNQKAEAKTRMTM | ||||||
Coiled coil | 898-928 | |||||
Sequence: RENLRPRKKALEDELEHKKEEQEMFFRMNEE | ||||||
Region | 930-951 | Disordered | ||||
Sequence: AGHPFPSNKPAKFYSFSSPEAS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length951
- Mass (Da)111,828
- Last updated2006-10-03 v1
- ChecksumBB08720CABE2960D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 343-357 | Basic and acidic residues | ||||
Sequence: ALGEKDKHTGKEHVG | ||||||
Compositional bias | 373-395 | Basic and acidic residues | ||||
Sequence: IHSQKRNHEGKNYPEHNRHDAVN | ||||||
Compositional bias | 425-479 | Polar residues | ||||
Sequence: EHGSAVSSNQRPKSSQSDRQSVELVPNGSFDSPTRYFTGWSKRDSDSGSNSASES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAMC01112142 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01112143 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01112144 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01112145 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC123019 EMBL· GenBank· DDBJ | AAI23020.1 EMBL· GenBank· DDBJ | mRNA |