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O95835

- LATS1_HUMAN

UniProt

O95835 - LATS1_HUMAN

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Protein

Serine/threonine-protein kinase LATS1

Gene

LATS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei734 – 7341ATP1 PublicationPROSITE-ProRule annotation
Active sitei828 – 8281Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi711 – 7199ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cytoplasmic sequestering of protein Source: BHF-UCL
  2. G2/M transition of mitotic cell cycle Source: UniProtKB
  3. hippo signaling Source: BHF-UCL
  4. hormone-mediated signaling pathway Source: UniProtKB
  5. keratinocyte differentiation Source: Ensembl
  6. mitotic nuclear division Source: UniProtKB-KW
  7. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  8. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  9. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  10. protein phosphorylation Source: UniProtKB
  11. regulation of actin filament polymerization Source: UniProtKB
  12. regulation of protein complex assembly Source: BHF-UCL
  13. sister chromatid segregation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118607. Signaling by Hippo.
SignaLinkiO95835.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase LATS1 (EC:2.7.11.1)
Alternative name(s):
Large tumor suppressor homolog 1
WARTS protein kinase
Short name:
h-warts
Gene namesi
Name:LATS1Imported
Synonyms:WARTSImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6514. LATS1.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi464 – 4641S → A: Abolishes phosphorylation by NUAK1 and NUAK2. 1 Publication
Mutagenesisi559 – 5591Y → F: Loss of interaction with YAP1. 1 Publication
Mutagenesisi734 – 7341K → A: Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA30301.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11301130Serine/threonine-protein kinase LATS1PRO_0000086232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461Phosphothreonine1 Publication
Modified residuei278 – 2781Phosphoserine1 Publication
Modified residuei464 – 4641Phosphoserine; by NUAK1 and NUAK22 Publications
Modified residuei613 – 6131PhosphoserineBy similarity
Modified residuei674 – 6741Phosphoserine1 Publication
Modified residuei909 – 9091Phosphoserine; by STK3/MST21 Publication
Modified residuei1079 – 10791Phosphothreonine; by STK3/MST21 Publication

Post-translational modificationi

Autophosphorylated and phosphorylated during M-phase of the cell cycle. Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079, which results in its activation. Phosphorylation at Ser-464 by NUAK1 and NUAK2 leads to decreased protein level and is required to regulate cellular senescence and cellular ploidy.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95835.
PaxDbiO95835.
PRIDEiO95835.

PTM databases

PhosphoSiteiO95835.

Expressioni

Tissue specificityi

Expressed in all adult tissues examined except for lung and kidney.1 Publication

Gene expression databases

BgeeiO95835.
CleanExiHS_LATS1.
ExpressionAtlasiO95835. baseline and differential.
GenevestigatoriO95835.

Organism-specific databases

HPAiHPA031804.

Interactioni

Subunit structurei

Complexes with CDK1 in early mitosis. LATS1-associated CDK1 has no mitotic cyclin partner and no apparent kinase activity. Binds phosphorylated ZYX, locating this protein to the mitotic spindle and suggesting a role for actin regulatory proteins during mitosis. Binds to and colocalizes with LIMK1 at the actomyosin contractile ring during cytokinesis. Interacts (via PPxY motif 2) with YAP1 (via WW domains). Interacts with MOB1A and MOB1B. Interacts with LIMD1, WTIP and AJUBA.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK1P064932EBI-444209,EBI-444308
LIMK1P536675EBI-444209,EBI-444403
MOB1AQ9H8S99EBI-444209,EBI-748229
MOB1BQ7L9L46EBI-444209,EBI-2558745
NF2P352404EBI-444209,EBI-1014472
Nf2P466625EBI-444209,EBI-644586From a different organism.
NUAK1O602852EBI-444209,EBI-1046789
VPRBPQ9Y4B64EBI-444209,EBI-1996353
WWTR1Q9GZV55EBI-444209,EBI-747743
YAP1P469375EBI-444209,EBI-1044059
ZYXQ1594210EBI-444209,EBI-444225

Protein-protein interaction databases

BioGridi114563. 72 interactions.
DIPiDIP-31516N.
IntActiO95835. 43 interactions.
MINTiMINT-2799169.

Structurei

3D structure databases

ProteinModelPortaliO95835.
SMRiO95835. Positions 95-142, 626-1046.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 14142UBAPROSITE-ProRule annotationAdd
BLAST
Domaini705 – 1010306Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1011 – 109080AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni526 – 655130Interaction with YAP1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi373 – 3764PPxY motif 1
Motifi556 – 5594PPxY motif 2

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000040002.
HOVERGENiHBG052311.
InParanoidiO95835.
KOiK08791.
OMAiAGFDEDM.
OrthoDBiEOG7BZVS1.
PhylomeDBiO95835.
TreeFamiTF351549.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR028741. LATS1/Warts.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PANTHERiPTHR24356:SF138. PTHR24356:SF138. 1 hit.
PfamiPF00069. Pkinase. 2 hits.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: O95835-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA
60 70 80 90 100
EHNMSKMSTE DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE
110 120 130 140 150
VNPQMLQDLQ AAGFDEDMVI QALQKTNNRS IEAAIEFISK MSYQDPRREQ
160 170 180 190 200
MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG SKESLVPQRH GPPLGESVAY
210 220 230 240 250
HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP QVRSVTPPPP
260 270 280 290 300
PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY
310 320 330 340 350
PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG
360 370 380 390 400
TGQTDFMIHQ NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY
410 420 430 440 450
TNGSIPQSMM VPNRNSHNME LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE
460 470 480 490 500
IPTWQPNIPV RSNSFNNPLG NRASHSANSQ PSATTVTAIT PAPIQQPVKS
510 520 530 540 550
MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV TVMPPVAEAP
560 570 580 590 600
NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV
610 620 630 640 650
DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV
660 670 680 690 700
LKSHQQRLHR KKQLENEMMR VGLSQDAQDQ MRKMLCQKES NYIRLKRAKM
710 720 730 740 750
DKSMFVKIKT LGIGAFGEVC LARKVDTKAL YATKTLRKKD VLLRNQVAHV
760 770 780 790 800
KAERDILAEA DNEWVVRLYY SFQDKDNLYF VMDYIPGGDM MSLLIRMGIF
810 820 830 840 850
PESLARFYIA ELTCAVESVH KMGFIHRDIK PDNILIDRDG HIKLTDFGLC
860 870 880 890 900
TGFRWTHDSK YYQSGDHPRQ DSMDFSNEWG DPSSCRCGDR LKPLERRAAR
910 920 930 940 950
QHQRCLAHSL VGTPNYIAPE VLLRTGYTQL CDWWSVGVIL FEMLVGQPPF
960 970 980 990 1000
LAQTPLETQM KVINWQTSLH IPPQAKLSPE ASDLIIKLCR GPEDRLGKNG
1010 1020 1030 1040 1050
ADEIKAHPFF KTIDFSSDLR QQSASYIPKI THPTDTSNFD PVDPDKLWSD
1060 1070 1080 1090 1100
DNEEENVNDT LNGWYKNGKH PEHAFYEFTF RRFFDDNGYP YNYPKPIEYE
1110 1120 1130
YINSQGSEQQ SDEDDQNTGS EIKNRDLVYV
Length:1,130
Mass (Da):126,870
Last modified:May 1, 1999 - v1
Checksum:i11CFBCD8FD87DCD8
GO
Isoform 2Curated (identifier: O95835-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     672-690: GLSQDAQDQMRKMLCQKES → KPFKMSIFILNHLFAWCLF
     691-1130: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:690
Mass (Da):76,193
Checksum:i7154097947DF44E8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961R → W.1 Publication
Corresponds to variant rs55945045 [ dbSNP | Ensembl ].
VAR_040660
Natural varianti204 – 2041S → G.1 Publication
Corresponds to variant rs34793526 [ dbSNP | Ensembl ].
VAR_040661
Natural varianti237 – 2371P → Q.1 Publication
Corresponds to variant rs56149740 [ dbSNP | Ensembl ].
VAR_040662
Natural varianti370 – 3701R → W.1 Publication
Corresponds to variant rs56348064 [ dbSNP | Ensembl ].
VAR_040663
Natural varianti531 – 5311P → S.1 Publication
Corresponds to variant rs55874734 [ dbSNP | Ensembl ].
VAR_040664
Natural varianti641 – 6411F → L.1 Publication
Corresponds to variant rs35163691 [ dbSNP | Ensembl ].
VAR_040665
Natural varianti669 – 6691M → I in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040666
Natural varianti806 – 8061R → P in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_040667
Natural varianti1000 – 10001G → S.1 Publication
Corresponds to variant rs56412005 [ dbSNP | Ensembl ].
VAR_040668

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei672 – 69019GLSQD…CQKES → KPFKMSIFILNHLFAWCLF in isoform 2. 1 PublicationVSP_051604Add
BLAST
Alternative sequencei691 – 1130440Missing in isoform 2. 1 PublicationVSP_051605Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104413 mRNA. Translation: AAD16882.1.
AF164041 mRNA. Translation: AAD50272.1.
BC002767 mRNA. Translation: AAH02767.1.
CCDSiCCDS34551.1. [O95835-1]
CCDS59040.1. [O95835-2]
RefSeqiNP_001257448.1. NM_001270519.1. [O95835-2]
NP_004681.1. NM_004690.3. [O95835-1]
UniGeneiHs.549084.

Genome annotation databases

EnsembliENST00000253339; ENSP00000253339; ENSG00000131023. [O95835-1]
ENST00000392273; ENSP00000444678; ENSG00000131023. [O95835-2]
ENST00000543571; ENSP00000437550; ENSG00000131023. [O95835-1]
GeneIDi9113.
KEGGihsa:9113.
UCSCiuc003qmu.2. human. [O95835-1]
uc003qmw.3. human. [O95835-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104413 mRNA. Translation: AAD16882.1 .
AF164041 mRNA. Translation: AAD50272.1 .
BC002767 mRNA. Translation: AAH02767.1 .
CCDSi CCDS34551.1. [O95835-1 ]
CCDS59040.1. [O95835-2 ]
RefSeqi NP_001257448.1. NM_001270519.1. [O95835-2 ]
NP_004681.1. NM_004690.3. [O95835-1 ]
UniGenei Hs.549084.

3D structure databases

ProteinModelPortali O95835.
SMRi O95835. Positions 95-142, 626-1046.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114563. 72 interactions.
DIPi DIP-31516N.
IntActi O95835. 43 interactions.
MINTi MINT-2799169.

Chemistry

BindingDBi O95835.
ChEMBLi CHEMBL6167.
GuidetoPHARMACOLOGYi 1515.

PTM databases

PhosphoSitei O95835.

Proteomic databases

MaxQBi O95835.
PaxDbi O95835.
PRIDEi O95835.

Protocols and materials databases

DNASUi 9113.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253339 ; ENSP00000253339 ; ENSG00000131023 . [O95835-1 ]
ENST00000392273 ; ENSP00000444678 ; ENSG00000131023 . [O95835-2 ]
ENST00000543571 ; ENSP00000437550 ; ENSG00000131023 . [O95835-1 ]
GeneIDi 9113.
KEGGi hsa:9113.
UCSCi uc003qmu.2. human. [O95835-1 ]
uc003qmw.3. human. [O95835-2 ]

Organism-specific databases

CTDi 9113.
GeneCardsi GC06M150023.
HGNCi HGNC:6514. LATS1.
HPAi HPA031804.
MIMi 603473. gene.
neXtProti NX_O95835.
PharmGKBi PA30301.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118994.
HOGENOMi HOG000040002.
HOVERGENi HBG052311.
InParanoidi O95835.
KOi K08791.
OMAi AGFDEDM.
OrthoDBi EOG7BZVS1.
PhylomeDBi O95835.
TreeFami TF351549.

Enzyme and pathway databases

Reactomei REACT_118607. Signaling by Hippo.
SignaLinki O95835.

Miscellaneous databases

GeneWikii LATS1.
GenomeRNAii 9113.
NextBioi 34157.
PROi O95835.
SOURCEi Search...

Gene expression databases

Bgeei O95835.
CleanExi HS_LATS1.
ExpressionAtlasi O95835. baseline and differential.
Genevestigatori O95835.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR028741. LATS1/Warts.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view ]
PANTHERi PTHR24356:SF138. PTHR24356:SF138. 1 hit.
Pfami PF00069. Pkinase. 2 hits.
PF00627. UBA. 1 hit.
[Graphical view ]
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human homologue of the Drosophila melanogaster lats tumour suppressor modulates CDC2 activity."
    Tao W., Zhang S., Turenchalk G.S., Stewart R.A., St John M.A., Chen W., Xu T.
    Nat. Genet. 21:177-181(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, INTERACTION WITH CDK1.
    Tissue: Fetal brainImported.
  2. "A human homolog of Drosophila warts tumor suppressor, h-warts, localized to mitotic apparatus and specifically phosphorylated during mitosis."
    Nishiyama Y., Hirota T., Morisaki T., Hara T., Marumoto T., Iida S., Makino K., Yamamoto H., Hiraoka T., Kitamura N., Saya H.
    FEBS Lett. 459:159-165(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: EndometriumImported.
  4. "Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor."
    Hirota T., Morisaki T., Nishiyama Y., Marumoto T., Tada K., Hara T., Masuko N., Inagaki M., Hatakeyama K., Saya H.
    J. Cell Biol. 149:1073-1086(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZYX.
  5. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Tumor suppressor WARTS ensures genomic integrity by regulating both mitotic progression and G1 tetraploidy checkpoint function."
    Iida S., Hirota T., Morisaki T., Marumoto T., Hara T., Kuninaka S., Honda S., Kosai K., Kawasuji M., Pallas D.C., Saya H.
    Oncogene 23:5266-5274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-734.
  7. "LATS1 tumour suppressor affects cytokinesis by inhibiting LIMK1."
    Yang X., Yu K., Hao Y., Li D.-M., Stewart R.A., Insogna K.L., Xu T.
    Nat. Cell Biol. 6:609-617(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LIMK1.
  8. "The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1."
    Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A., Nigg E.A., Sillje H.H.W.
    Oncogene 24:2076-2086(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-909 AND THR-1079.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
    Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
    J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YAP1, MUTAGENESIS OF TYR-559.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-278 AND SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Ajuba LIM proteins are negative regulators of the Hippo signaling pathway."
    Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B., Longmore G.D.
    Curr. Biol. 20:657-662(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIMD1; WTIP AND AJUBA.
  17. "Molecular characterization of human homologs of yeast MOB1."
    Chow A., Hao Y., Yang X.
    Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOB1A AND MOB1B.
  18. Cited for: FUNCTION, PHOSPHORYLATION AT SER-464, MUTAGENESIS OF SER-464.
  19. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-96; GLY-204; GLN-237; TRP-370; SER-531; LEU-641; ILE-669; PRO-806 AND SER-1000.

Entry informationi

Entry nameiLATS1_HUMAN
AccessioniPrimary (citable) accession number: O95835
Secondary accession number(s): Q6PKD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3