O95835 · LATS1_HUMAN
- ProteinSerine/threonine-protein kinase LATS1
- GeneLATS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1130 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase LATS1
- 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 accessionO95835
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_040660 | 96 | in dbSNP:rs55945045 | |||
Sequence: R → W | ||||||
Natural variant | VAR_040661 | 204 | in dbSNP:rs34793526 | |||
Sequence: S → G | ||||||
Natural variant | VAR_040662 | 237 | in dbSNP:rs56149740 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_040663 | 370 | in dbSNP:rs56348064 | |||
Sequence: R → W | ||||||
Mutagenesis | 464 | Abolishes phosphorylation by NUAK1 and NUAK2. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_040664 | 531 | in dbSNP:rs55874734 | |||
Sequence: P → S | ||||||
Mutagenesis | 559 | Loss of interaction with YAP1. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_040665 | 641 | in dbSNP:rs35163691 | |||
Sequence: F → L | ||||||
Natural variant | VAR_040666 | 669 | in a lung adenocarcinoma sample; somatic mutation; dbSNP:rs1390558952 | |||
Sequence: M → I | ||||||
Mutagenesis | 734 | Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_040667 | 806 | in a lung large cell carcinoma sample; somatic mutation | |||
Sequence: R → P | ||||||
Natural variant | VAR_040668 | 1000 | in dbSNP:rs56412005 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,367 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086232 | 1-1130 | UniProt | Serine/threonine-protein kinase LATS1 | |||
Sequence: MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKFGTHHKALQEIRNSLLPFANETNSSRSTSEVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSYQDPRREQMAAAAARPINASMKPGNVQQSVNRKQSWKGSKESLVPQRHGPPLGESVAYHSESPNSQTDVGRPLSGSGISAFVQAHPSNGQRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEPNSQTKRYSGNMEYVISRISPVPPGAWQEGYPPPPLNTSPMNPPNQGQRGISSVPVGRQPIIMQSSSKFNFPSGRPGMQNGTGQTDFMIHQNVVPAGTVNRQPPPPYPLTAANGQSPSALQTGGSAAPSSYTNGSIPQSMMVPNRNSHNMELYNISVPGLQTNWPQSSSAPAQSSPSSGHEIPTWQPNIPVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQSASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFFDDNGYPYNYPKPIEYEYINSQGSEQQSDEDDQNTGSEIKNRDLVYV | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 246 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 246 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 278 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 462 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 464 | UniProt | Phosphoserine; by NUAK1 and NUAK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 464 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 573 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 575 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 613 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 613 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 635 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 674 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 909 | UniProt | Phosphoserine; by STK3/MST2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 909 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1079 | UniProt | Phosphothreonine; by STK3/MST2 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1111 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079, which results in its activation (PubMed:15688006).
Phosphorylated by MAP4Ks; in parallel to STK3/MST2 and resulting to its activation (PubMed:26437443).
Phosphorylation at Ser-464 by NUAK1 and NUAK2 leads to decreased protein level and is required to regulate cellular senescence and cellular ploidy (PubMed:19927127).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
LATS1-associated CDK1 has no mitotic cyclin partner and no apparent kinase activity (PubMed:9988268).
Binds phosphorylated ZYX, locating this protein to the mitotic spindle and suggesting a role for actin regulatory proteins during mitosis (PubMed:10831611).
Binds to and colocalizes with LIMK1 at the actomyosin contractile ring during cytokinesis (PubMed:15220930).
Interacts (via PPxY motif 2) with YAP1 (via WW domains) (PubMed:18158288).
Interacts with MOB1A and MOB1B (PubMed:19739119).
Interacts with LIMD1, WTIP and AJUBA (PubMed:20303269).
Interacts with ESR1, DCAF1 and DCAF13; probably recruits DCAF1 and DCAF13 to ESR1 to promote ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:28068668).
Interacts with STK3/MST2; this interaction is inhibited in the presence of DLG5 (PubMed:28087714).
Interacts with SCRIB in the presence of DLG5 (PubMed:28169360).
Interacts with WWTR1/TAZ (By similarity).
Interacts with WWC1, WWC2 and WWC3 (via their WW domains) (PubMed:24682284).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95835 | CDK1 P06493 | 3 | EBI-444209, EBI-444308 | |
BINARY | O95835 | CDK2 P24941 | 4 | EBI-444209, EBI-375096 | |
BINARY | O95835 | DCAF1 Q9Y4B6 | 4 | EBI-444209, EBI-1996353 | |
BINARY | O95835 | ESR1 P03372 | 2 | EBI-444209, EBI-78473 | |
BINARY | O95835 | LIMK1 P53667 | 5 | EBI-444209, EBI-444403 | |
BINARY | O95835 | MOB1A Q9H8S9 | 9 | EBI-444209, EBI-748229 | |
BINARY | O95835 | MOB1B Q7L9L4 | 9 | EBI-444209, EBI-2558745 | |
BINARY | O95835 | NF2 P35240 | 4 | EBI-444209, EBI-1014472 | |
XENO | O95835 | Nf2 P46662 | 5 | EBI-444209, EBI-644586 | |
BINARY | O95835 | NUAK1 O60285 | 2 | EBI-444209, EBI-1046789 | |
BINARY | O95835 | SIAH2 O43255 | 2 | EBI-444209, EBI-948141 | |
BINARY | O95835 | STK11 Q15831 | 2 | EBI-444209, EBI-306838 | |
BINARY | O95835 | WWTR1 Q9GZV5 | 5 | EBI-444209, EBI-747743 | |
BINARY | O95835 | YAP1 P46937 | 10 | EBI-444209, EBI-1044059 | |
BINARY | O95835 | ZYX Q15942 | 10 | EBI-444209, EBI-444225 | |
BINARY | O95835-2 | ARPC3 O15145 | 3 | EBI-17978514, EBI-351829 | |
BINARY | O95835-2 | UBQLN2 Q9UHD9 | 3 | EBI-17978514, EBI-947187 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-71 | Disordered | ||||
Sequence: MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKF | ||||||
Compositional bias | 17-38 | Polar residues | ||||
Sequence: TFPASNYTVSSRQMLQEIRESL | ||||||
Compositional bias | 39-59 | Basic and acidic residues | ||||
Sequence: RNLSKPSDAAKAEHNMSKMST | ||||||
Domain | 100-141 | UBA | ||||
Sequence: EVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKM | ||||||
Region | 149-276 | Disordered | ||||
Sequence: EQMAAAAARPINASMKPGNVQQSVNRKQSWKGSKESLVPQRHGPPLGESVAYHSESPNSQTDVGRPLSGSGISAFVQAHPSNGQRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEPNSQTKR | ||||||
Compositional bias | 163-183 | Polar residues | ||||
Sequence: MKPGNVQQSVNRKQSWKGSKE | ||||||
Compositional bias | 200-215 | Polar residues | ||||
Sequence: YHSESPNSQTDVGRPL | ||||||
Compositional bias | 232-270 | Pro residues | ||||
Sequence: QRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEP | ||||||
Region | 294-321 | Disordered | ||||
Sequence: GAWQEGYPPPPLNTSPMNPPNQGQRGIS | ||||||
Compositional bias | 295-310 | Pro residues | ||||
Sequence: AWQEGYPPPPLNTSPM | ||||||
Region | 365-405 | Disordered | ||||
Sequence: AGTVNRQPPPPYPLTAANGQSPSALQTGGSAAPSSYTNGSI | ||||||
Motif | 373-376 | PPxY motif 1 | ||||
Sequence: PPPY | ||||||
Compositional bias | 381-405 | Polar residues | ||||
Sequence: ANGQSPSALQTGGSAAPSSYTNGSI | ||||||
Region | 432-484 | Disordered | ||||
Sequence: NWPQSSSAPAQSSPSSGHEIPTWQPNIPVRSNSFNNPLGNRASHSANSQPSAT | ||||||
Compositional bias | 515-537 | Polar residues | ||||
Sequence: THPSWIPQPIQTVQPSPFPEGTA | ||||||
Region | 515-631 | Disordered | ||||
Sequence: THPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRI | ||||||
Region | 526-655 | Interaction with YAP1 | ||||
Sequence: TVQPSPFPEGTASNVTVMPPVAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQ | ||||||
Compositional bias | 549-565 | Pro residues | ||||
Sequence: APNYQGPPPPYPKHLLH | ||||||
Motif | 556-559 | PPxY motif 2 | ||||
Sequence: PPPY | ||||||
Compositional bias | 583-631 | Basic and acidic residues | ||||
Sequence: DQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRI | ||||||
Domain | 705-1010 | Protein kinase | ||||
Sequence: FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFF | ||||||
Domain | 1011-1090 | AGC-kinase C-terminal | ||||
Sequence: KTIDFSSDLRQQSASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFFDDNGYP | ||||||
Region | 1104-1130 | Disordered | ||||
Sequence: SQGSEQQSDEDDQNTGSEIKNRDLVYV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O95835-1
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
- Length1,130
- Mass (Da)126,870
- Last updated1999-05-01 v1
- Checksum11CFBCD8FD87DCD8
O95835-2
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-38 | Polar residues | ||||
Sequence: TFPASNYTVSSRQMLQEIRESL | ||||||
Compositional bias | 39-59 | Basic and acidic residues | ||||
Sequence: RNLSKPSDAAKAEHNMSKMST | ||||||
Compositional bias | 163-183 | Polar residues | ||||
Sequence: MKPGNVQQSVNRKQSWKGSKE | ||||||
Compositional bias | 200-215 | Polar residues | ||||
Sequence: YHSESPNSQTDVGRPL | ||||||
Compositional bias | 232-270 | Pro residues | ||||
Sequence: QRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEP | ||||||
Compositional bias | 295-310 | Pro residues | ||||
Sequence: AWQEGYPPPPLNTSPM | ||||||
Compositional bias | 381-405 | Polar residues | ||||
Sequence: ANGQSPSALQTGGSAAPSSYTNGSI | ||||||
Compositional bias | 515-537 | Polar residues | ||||
Sequence: THPSWIPQPIQTVQPSPFPEGTA | ||||||
Compositional bias | 549-565 | Pro residues | ||||
Sequence: APNYQGPPPPYPKHLLH | ||||||
Compositional bias | 583-631 | Basic and acidic residues | ||||
Sequence: DQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRI | ||||||
Alternative sequence | VSP_051604 | 672-690 | in isoform 2 | |||
Sequence: GLSQDAQDQMRKMLCQKES → KPFKMSIFILNHLFAWCLF | ||||||
Alternative sequence | VSP_051605 | 691-1130 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF104413 EMBL· GenBank· DDBJ | AAD16882.1 EMBL· GenBank· DDBJ | mRNA | ||
AF164041 EMBL· GenBank· DDBJ | AAD50272.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002767 EMBL· GenBank· DDBJ | AAH02767.1 EMBL· GenBank· DDBJ | mRNA |