O94804 · STK10_HUMAN
- ProteinSerine/threonine-protein kinase 10
- GeneSTK10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids968 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.
Miscellaneous
Inhibition by erlotinib, an orally administered EGFR tyrosine kinase inhibitor used for treatment, enhances STK10-dependent lymphocytic responses, possibly leading to the aggravation of skin inflammation observed upon treatment by erlotinib.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Inhibited by the pyrrole-indolinone inhibitor SU11274 (K00593): intercalates between the ATP-binding Lys-65 and alpha-C glutamate (Glu-81), resulting in a partial disordering of the lysine side chain. Also specifically inhibited by erlotinib. Slightly inhibited by gefitinib.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | plasma membrane | |
Cellular Component | specific granule membrane | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | lymphocyte aggregation | |
Biological Process | protein autophosphorylation | |
Biological Process | protein phosphorylation | |
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
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94804
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Testicular germ cell tumor (TGCT)
- Note
- DescriptionA common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
- See alsoMIM:273300
Natural variants in TGCT
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_023827 | 277 | K>E | in TGCT; somatic mutation; dbSNP:rs757545210 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 65 | Loss of kinase activity. | ||||
Sequence: K → I | ||||||
Natural variant | VAR_041131 | 268 | in dbSNP:rs35826078 | |||
Sequence: R → C | ||||||
Natural variant | VAR_023827 | 277 | in TGCT; somatic mutation; dbSNP:rs757545210 | |||
Sequence: K → E | ||||||
Natural variant | VAR_041132 | 322 | in dbSNP:rs56214442 | |||
Sequence: R → W | ||||||
Natural variant | VAR_041133 | 336 | in dbSNP:rs55972616 | |||
Sequence: T → I | ||||||
Natural variant | VAR_041134 | 467 | in dbSNP:rs56063773 | |||
Sequence: N → S | ||||||
Natural variant | VAR_051671 | 480 | in dbSNP:rs34505340 | |||
Sequence: P → L | ||||||
Natural variant | VAR_051672 | 520 | in dbSNP:rs17074311 | |||
Sequence: P → L | ||||||
Natural variant | VAR_041135 | 710 | in dbSNP:rs34936670 | |||
Sequence: M → T | ||||||
Natural variant | VAR_041136 | 853 | in dbSNP:rs56066852 | |||
Sequence: S → L | ||||||
Natural variant | VAR_041137 | 905 | in dbSNP:rs55791916 | |||
Sequence: S → T | ||||||
Natural variant | VAR_051673 | 942 | in dbSNP:rs1128204 | |||
Sequence: S → N | ||||||
Natural variant | VAR_041138 | 947 | in dbSNP:rs56355550 | |||
Sequence: C → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,098 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_0000086697 | 1-968 | UniProt | Serine/threonine-protein kinase 10 | |||
Sequence: MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNEVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYHDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHSKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLEHPFVSSITSNKALRELVAEAKAEVMEEIEDGRDEGEEEDAVDAASTLENHTQNSSEVSPPSLNADKPLEESPSTPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVAPGNENGLAVPVPLRKSRPVSMDARIQVAQEKQVAEQGGDLSPAANRSQKASQSRPNSSALETLGGEKLANGSLEPPAQAAPGPSKRDSDCSSLCTSESMDYGTNLSTDLSLNKEMGSLSIKDPKLYKKTLKRTRKFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSNKHELQLEQMHKRFEQEINAKKKFFDTELENLERQQKQQVEKMEQDHAVRRREEARRIRLEQDRDYTRFQEQLKLMKKEVKNEVEKLPRQQRKESMKQKMEEHTQKKQLLDRDFVAKQKEDLELAMKRLTTDNRREICDKERECLMKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKVRQQQEKARLPKIQRSEGKTRMAMYKKSLHINGGGSAAEQREKIKQFSQQEEKRQKSERLQQQQKHENQMRDMLAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQNLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAECPNPSTPSKAAKFFPYSSADAS | |||||||
Modified residue | 13 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 20 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 185 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 191 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 438 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 448 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 450 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 450 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 454 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 454 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 455 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 469 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 485 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 485 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 514 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 514 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 549 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 952 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 952 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 954 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 962 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Autophosphorylates following homodimerization, leading to activation of the protein.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in rapidly proliferating tissues (spleen, placenta, and peripheral blood leukocytes). Also expressed in brain, heart, skeletal muscle, colon, thymus, kidney, liver, small intestine and lung.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer; homodimerization is required for activation segment autophosphorylation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94804 | STK10 O94804 | 3 | EBI-3951541, EBI-3951541 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-294 | Protein kinase | ||||
Sequence: WEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYHDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHSKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLEHPFV | ||||||
Region | 175-224 | Activation segment | ||||
Sequence: DFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLG | ||||||
Compositional bias | 337-351 | Polar residues | ||||
Sequence: LENHTQNSSEVSPPS | ||||||
Region | 337-411 | Disordered | ||||
Sequence: LENHTQNSSEVSPPSLNADKPLEESPSTPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVAPGNENGLAVPVPLR | ||||||
Compositional bias | 363-397 | Polar residues | ||||
Sequence: STPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVA | ||||||
Region | 425-490 | Disordered | ||||
Sequence: AQEKQVAEQGGDLSPAANRSQKASQSRPNSSALETLGGEKLANGSLEPPAQAAPGPSKRDSDCSSL | ||||||
Compositional bias | 438-457 | Polar residues | ||||
Sequence: SPAANRSQKASQSRPNSSAL | ||||||
Coiled coil | 573-947 | |||||
Sequence: QKEEHRNQTQLSNKHELQLEQMHKRFEQEINAKKKFFDTELENLERQQKQQVEKMEQDHAVRRREEARRIRLEQDRDYTRFQEQLKLMKKEVKNEVEKLPRQQRKESMKQKMEEHTQKKQLLDRDFVAKQKEDLELAMKRLTTDNRREICDKERECLMKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKVRQQQEKARLPKIQRSEGKTRMAMYKKSLHINGGGSAAEQREKIKQFSQQEEKRQKSERLQQQQKHENQMRDMLAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQNLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAEC | ||||||
Region | 668-690 | Disordered | ||||
Sequence: VEKLPRQQRKESMKQKMEEHTQK | ||||||
Region | 827-865 | Disordered | ||||
Sequence: INGGGSAAEQREKIKQFSQQEEKRQKSERLQQQQKHENQ | ||||||
Compositional bias | 840-862 | Basic and acidic residues | ||||
Sequence: IKQFSQQEEKRQKSERLQQQQKH | ||||||
Region | 910-929 | Disordered | ||||
Sequence: LKEWRDKLRPRKKALEEDLN | ||||||
Region | 944-968 | Disordered | ||||
Sequence: EAECPNPSTPSKAAKFFPYSSADAS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length968
- Mass (Da)112,135
- Last updated1999-05-01 v1
- Checksum15E245193ECC553D
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YB71 | H0YB71_HUMAN | STK10 | 281 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 62 | in Ref. 5; AAH70077 | ||||
Sequence: A → V | ||||||
Sequence conflict | 136 | in Ref. 5; AAH70077 | ||||
Sequence: V → E | ||||||
Sequence conflict | 317 | in Ref. 5; AAH70077 | ||||
Sequence: E → G | ||||||
Compositional bias | 337-351 | Polar residues | ||||
Sequence: LENHTQNSSEVSPPS | ||||||
Compositional bias | 363-397 | Polar residues | ||||
Sequence: STPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVA | ||||||
Compositional bias | 438-457 | Polar residues | ||||
Sequence: SPAANRSQKASQSRPNSSAL | ||||||
Compositional bias | 840-862 | Basic and acidic residues | ||||
Sequence: IKQFSQQEEKRQKSERLQQQQKH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB015718 EMBL· GenBank· DDBJ | BAA35073.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022960 EMBL· GenBank· DDBJ | BAG51143.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK313350 EMBL· GenBank· DDBJ | BAG36152.1 EMBL· GenBank· DDBJ | mRNA | ||
AC024561 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471062 EMBL· GenBank· DDBJ | EAW61439.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC070077 EMBL· GenBank· DDBJ | AAH70077.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133081 EMBL· GenBank· DDBJ | CAB61400.1 EMBL· GenBank· DDBJ | mRNA |