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O95835 (LATS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LATS1
Synonyms:WARTS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1130 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4 Ref.6 Ref.7 Ref.10 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.2 Ref.6

Cofactor

Magnesium. Ref.2 Ref.6

Subunit structure

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. Ref.1 Ref.4 Ref.7 Ref.10 Ref.16 Ref.17

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis. Ref.2

Tissue specificity

Expressed in all adult tissues examined except for lung and kidney. Ref.2

Post-translational modification

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. Ref.1 Ref.2 Ref.6 Ref.8 Ref.18

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasmic sequestering of protein

Inferred from mutant phenotype PubMed 20412773. Source: BHF-UCL

hippo signaling

Inferred from direct assay PubMed 20412773. Source: BHF-UCL

hormone-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 20412773. Source: BHF-UCL

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 20412773. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of actin filament polymerization

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of protein complex assembly

Inferred from mutant phenotype PubMed 20412773. Source: BHF-UCL

sister chromatid segregation

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle pole

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.2. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.17Ref.16. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.7Ref.18. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: 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.
Isoform 2 (identifier: O95835-2)

The sequence of this isoform differs from the canonical sequence as follows:
     672-690: GLSQDAQDQMRKMLCQKES → KPFKMSIFILNHLFAWCLF
     691-1130: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11301130Serine/threonine-protein kinase LATS1
PRO_0000086232

Regions

Domain100 – 14142UBA
Domain705 – 1010306Protein kinase
Domain1011 – 109080AGC-kinase C-terminal
Nucleotide binding711 – 7199ATP By similarity UniProtKB P22612
Region526 – 655130Interaction with YAP1
Motif373 – 3764PPxY motif 1
Motif556 – 5594PPxY motif 2

Sites

Active site8281Proton acceptor By similarity UniProtKB P22612
Binding site7341ATP Ref.6

Amino acid modifications

Modified residue2461Phosphothreonine Ref.12
Modified residue2781Phosphoserine Ref.12
Modified residue4641Phosphoserine; by NUAK1 and NUAK2 Ref.12 Ref.18
Modified residue6131Phosphoserine By similarity
Modified residue6741Phosphoserine Ref.9
Modified residue9091Phosphoserine; by STK3/MST2 Ref.8
Modified residue10791Phosphothreonine; by STK3/MST2 Ref.8

Natural variations

Alternative sequence672 – 69019GLSQD…CQKES → KPFKMSIFILNHLFAWCLF in isoform 2.
VSP_051604
Alternative sequence691 – 1130440Missing in isoform 2.
VSP_051605
Natural variant961R → W. Ref.19
Corresponds to variant rs55945045 [ dbSNP | Ensembl ].
VAR_040660
Natural variant2041S → G. Ref.19
Corresponds to variant rs34793526 [ dbSNP | Ensembl ].
VAR_040661
Natural variant2371P → Q. Ref.19
Corresponds to variant rs56149740 [ dbSNP | Ensembl ].
VAR_040662
Natural variant3701R → W. Ref.19
Corresponds to variant rs56348064 [ dbSNP | Ensembl ].
VAR_040663
Natural variant5311P → S. Ref.19
Corresponds to variant rs55874734 [ dbSNP | Ensembl ].
VAR_040664
Natural variant6411F → L. Ref.19
Corresponds to variant rs35163691 [ dbSNP | Ensembl ].
VAR_040665
Natural variant6691M → I in a lung adenocarcinoma sample; somatic mutation. Ref.19
VAR_040666
Natural variant8061R → P in a lung large cell carcinoma sample; somatic mutation. Ref.19
VAR_040667
Natural variant10001G → S. Ref.19
Corresponds to variant rs56412005 [ dbSNP | Ensembl ].
VAR_040668

Experimental info

Mutagenesis4641S → A: Abolishes phosphorylation by NUAK1 and NUAK2. Ref.18
Mutagenesis5591Y → F: Loss of interaction with YAP1. Ref.10
Mutagenesis7341K → A: Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 11CFBCD8FD87DCD8

FASTA1,130126,870
        10         20         30         40         50         60 
MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA EHNMSKMSTE 

        70         80         90        100        110        120 
DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE VNPQMLQDLQ AAGFDEDMVI 

       130        140        150        160        170        180 
QALQKTNNRS IEAAIEFISK MSYQDPRREQ MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG 

       190        200        210        220        230        240 
SKESLVPQRH GPPLGESVAY HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP 

       250        260        270        280        290        300 
QVRSVTPPPP PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY 

       310        320        330        340        350        360 
PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG TGQTDFMIHQ 

       370        380        390        400        410        420 
NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY TNGSIPQSMM VPNRNSHNME 

       430        440        450        460        470        480 
LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE IPTWQPNIPV RSNSFNNPLG NRASHSANSQ 

       490        500        510        520        530        540 
PSATTVTAIT PAPIQQPVKS MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV 

       550        560        570        580        590        600 
TVMPPVAEAP NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV 

       610        620        630        640        650        660 
DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV LKSHQQRLHR 

       670        680        690        700        710        720 
KKQLENEMMR VGLSQDAQDQ MRKMLCQKES NYIRLKRAKM DKSMFVKIKT LGIGAFGEVC 

       730        740        750        760        770        780 
LARKVDTKAL YATKTLRKKD VLLRNQVAHV KAERDILAEA DNEWVVRLYY SFQDKDNLYF 

       790        800        810        820        830        840 
VMDYIPGGDM MSLLIRMGIF PESLARFYIA ELTCAVESVH KMGFIHRDIK PDNILIDRDG 

       850        860        870        880        890        900 
HIKLTDFGLC TGFRWTHDSK YYQSGDHPRQ DSMDFSNEWG DPSSCRCGDR LKPLERRAAR 

       910        920        930        940        950        960 
QHQRCLAHSL VGTPNYIAPE VLLRTGYTQL CDWWSVGVIL FEMLVGQPPF LAQTPLETQM 

       970        980        990       1000       1010       1020 
KVINWQTSLH IPPQAKLSPE ASDLIIKLCR GPEDRLGKNG ADEIKAHPFF KTIDFSSDLR 

      1030       1040       1050       1060       1070       1080 
QQSASYIPKI THPTDTSNFD PVDPDKLWSD DNEEENVNDT LNGWYKNGKH PEHAFYEFTF 

      1090       1100       1110       1120       1130 
RRFFDDNGYP YNYPKPIEYE YINSQGSEQQ SDEDDQNTGS EIKNRDLVYV 

« Hide

Isoform 2 [UniParc].

Checksum: 7154097947DF44E8
Show »

FASTA69076,193

References

« Hide 'large scale' references
[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 brain.
[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: Endometrium.
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Regulation of ploidy and senescence by the AMPK-related kinase NUAK1."
Humbert N., Navaratnam N., Augert A., Da Costa M., Martien S., Wang J., Martinez D., Abbadie C., Carling D., de Launoit Y., Gil J., Bernard D.
EMBO J. 29:376-386(2010) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF104413 mRNA. Translation: AAD16882.1.
AF164041 mRNA. Translation: AAD50272.1.
BC002767 mRNA. Translation: AAH02767.1.
CCDSCCDS34551.1. [O95835-1]
CCDS59040.1. [O95835-2]
RefSeqNP_001257448.1. NM_001270519.1. [O95835-2]
NP_004681.1. NM_004690.3. [O95835-1]
UniGeneHs.549084.

3D structure databases

ProteinModelPortalO95835.
SMRO95835. Positions 95-142, 626-1046.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114563. 72 interactions.
DIPDIP-31516N.
IntActO95835. 40 interactions.
MINTMINT-2799169.

Chemistry

BindingDBO95835.
ChEMBLCHEMBL6167.
GuidetoPHARMACOLOGY1515.

PTM databases

PhosphoSiteO95835.

Proteomic databases

MaxQBO95835.
PaxDbO95835.
PRIDEO95835.

Protocols and materials databases

DNASU9113.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253339; ENSP00000253339; ENSG00000131023. [O95835-1]
ENST00000392273; ENSP00000444678; ENSG00000131023. [O95835-2]
ENST00000543571; ENSP00000437550; ENSG00000131023. [O95835-1]
GeneID9113.
KEGGhsa:9113.
UCSCuc003qmu.2. human. [O95835-1]
uc003qmw.3. human. [O95835-2]

Organism-specific databases

CTD9113.
GeneCardsGC06M150023.
HGNCHGNC:6514. LATS1.
HPAHPA031804.
MIM603473. gene.
neXtProtNX_O95835.
PharmGKBPA30301.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000040002.
HOVERGENHBG052311.
InParanoidO95835.
KOK08791.
OMAAGFDEDM.
OrthoDBEOG7BZVS1.
PhylomeDBO95835.
TreeFamTF351549.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkO95835.

Gene expression databases

ArrayExpressO95835.
BgeeO95835.
CleanExHS_LATS1.
GenevestigatorO95835.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR028741. LATS1/Warts.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PANTHERPTHR24356:SF138. PTHR24356:SF138. 1 hit.
PfamPF00069. Pkinase. 2 hits.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLATS1.
GenomeRNAi9113.
NextBio34157.
PROO95835.
SOURCESearch...

Entry information

Entry nameLATS1_HUMAN
AccessionPrimary (citable) accession number: O95835
Secondary accession number(s): Q6PKD0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM