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Q9NRM7

- LATS2_HUMAN

UniProt

Q9NRM7 - LATS2_HUMAN

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Protein
Serine/threonine-protein kinase LATS2
Gene
LATS2, KPM
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 LATS2 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 centrosome duplication, maintenance of mitotic fidelity and genomic stability. Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity. Negative regulator of the androgen receptor. Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities. This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei697 – 6971ATP1 Publication
Active sitei791 – 7911Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi674 – 782109ATP By similarityBy similarity
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: UniProtKB
  2. cellular protein localization Source: Ensembl
  3. hippo signaling Source: BHF-UCL
  4. hormone-mediated signaling pathway Source: UniProtKB
  5. intracellular signal transduction Source: UniProtKB
  6. keratinocyte differentiation Source: Ensembl
  7. mitotic nuclear division Source: UniProtKB-KW
  8. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  9. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  10. protein phosphorylation Source: UniProtKB
  11. regulation of organ growth Source: Ensembl
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.
SignaLinkiQ9NRM7.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase LATS2 (EC:2.7.11.1)
Alternative name(s):
Kinase phosphorylated during mitosis protein
Large tumor suppressor homolog 2
Serine/threonine-protein kinase kpm
Warts-like kinase
Gene namesi
Name:LATS2
Synonyms:KPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:6515. LATS2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasm. Cytoplasmcytoskeletonspindle pole. Nucleus
Note: Colocalizes with AURKA at the centrosomes during interphase, early prophase and cytokinesis. Migrates to the spindle poles during mitosis, and to the midbody during cytokinesis. Translocates to the nucleus upon mitotic stress by nocodazole treatment.3 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
  4. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831S → C: Fails to localize at the centromere during interphase. 1 Publication
Mutagenesisi83 – 831S → E: Fails to localize at the centromere during interphase. 1 Publication
Mutagenesisi697 – 6971K → A: Loss of kinase activity, autophosphorylation and tumor suppressor activity. 2 Publications
Mutagenesisi872 – 8721S → A: Loss of tumor suppressor activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA30302.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10881088Serine/threonine-protein kinase LATS2
PRO_0000086234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831Phosphoserine; by AURKA1 Publication
Modified residuei279 – 2791Phosphothreonine1 Publication
Modified residuei1041 – 10411Phosphothreonine1 Publication

Post-translational modificationi

Autophosphorylated and phosphorylated during M-phase and the G1/S-phase of the cell cycle. Phosphorylated and activated by STK3/MST2.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRM7.
PaxDbiQ9NRM7.
PRIDEiQ9NRM7.

PTM databases

PhosphoSiteiQ9NRM7.

Expressioni

Tissue specificityi

Expressed at high levels in heart and skeletal muscle and at lower levels in all other tissues examined.2 Publications

Gene expression databases

BgeeiQ9NRM7.
CleanExiHS_LATS2.
GenevestigatoriQ9NRM7.

Organism-specific databases

HPAiHPA039191.

Interactioni

Subunit structurei

Interacts with and is phosphorylated by AURKA. Binds to AR. Interacts with AJUBA during mitosis and this complex regulates organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome. Interacts (via PPxY motif) with YAP1 (via WW domains). Interacts with MOB1A and MOB1B. Interacts with LIMD1, WTIP and AJUBA. Interacts with SNAI1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AJUBAQ96IF16EBI-3506895,EBI-949782
MOB1AQ9H8S94EBI-3506895,EBI-748229
MOB1BQ7L9L43EBI-3506895,EBI-2558745

Protein-protein interaction databases

BioGridi117727. 144 interactions.
IntActiQ9NRM7. 8 interactions.
MINTiMINT-1772003.
STRINGi9606.ENSP00000372035.

Structurei

3D structure databases

ProteinModelPortaliQ9NRM7.
SMRiQ9NRM7. Positions 92-139, 640-1042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 13942UBA
Add
BLAST
Domaini668 – 973306Protein kinase
Add
BLAST
Domaini974 – 105279AGC-kinase C-terminal
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi515 – 5184PPxY motif

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000040002.
HOVERGENiHBG052311.
InParanoidiQ9NRM7.
KOiK08791.
OMAiGSHIRQD.
OrthoDBiEOG7BZVS1.
PhylomeDBiQ9NRM7.
TreeFamiTF351549.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR028742. LATS2.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PANTHERiPTHR24356:SF149. PTHR24356:SF149. 1 hit.
PfamiPF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 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.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NRM7-1 [UniParc]FASTAAdd to Basket

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MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSVQGLPAG PNSDTSLDAK     50
VLGSKDATRQ QQQMRATPKF GPYQKALREI RYSLLPFANE SGTSAAAEVN 100
RQMLQELVNA GCDQEMAGRA LKQTGSRSIE AALEYISKMG YLDPRNEQIV 150
RVIKQTSPGK GLMPTPVTRR PSFEGTGDSF ASYHQLSGTP YEGPSFGADG 200
PTALEEMPRP YVDYLFPGVG PHGPGHQHQH PPKGYGASVE AAGAHFPLQG 250
AHYGRPHLLV PGEPLGYGVQ RSPSFQSKTP PETGGYASLP TKGQGGPPGA 300
GLAFPPPAAG LYVPHPHHKQ AGPAAHQLHV LGSRSQVFAS DSPPQSLLTP 350
SRNSLNVDLY ELGSTSVQQW PAATLARRDS LQKPGLEAPP RAHVAFRPDC 400
PVPSRTNSFN SHQPRPGPPG KAEPSLPAPN TVTAVTAAHI LHPVKSVRVL 450
RPEPQTAVGP SHPAWVPAPA PAPAPAPAPA AEGLDAKEEH ALALGGAGAF 500
PLDVEYGGPD RRCPPPPYPK HLLLRSKSEQ YDLDSLCAGM EQSLRAGPNE 550
PEGGDKSRKS AKGDKGGKDK KQIQTSPVPV RKNSRDEEKR ESRIKSYSPY 600
AFKFFMEQHV ENVIKTYQQK VNRRLQLEQE MAKAGLCEAE QEQMRKILYQ 650
KESNYNRLKR AKMDKSMFVK IKTLGIGAFG EVCLACKVDT HALYAMKTLR 700
KKDVLNRNQV AHVKAERDIL AEADNEWVVK LYYSFQDKDS LYFVMDYIPG 750
GDMMSLLIRM EVFPEHLARF YIAELTLAIE SVHKMGFIHR DIKPDNILID 800
LDGHIKLTDF GLCTGFRWTH NSKYYQKGSH VRQDSMEPSD LWDDVSNCRC 850
GDRLKTLEQR ARKQHQRCLA HSLVGTPNYI APEVLLRKGY TQLCDWWSVG 900
VILFEMLVGQ PPFLAPTPTE TQLKVINWEN TLHIPAQVKL SPEARDLITK 950
LCCSADHRLG RNGADDLKAH PFFSAIDFSS DIRKQPAPYV PTISHPMDTS 1000
NFDPVDEESP WNDASEGSTK AWDTLTSPNN KHPEHAFYEF TFRRFFDDNG 1050
YPFRCPKPSG AEASQAESSD LESSDLVDQT EGCQPVYV 1088
Length:1,088
Mass (Da):120,136
Last modified:November 4, 2008 - v2
Checksum:i2866F6B75637AD36
GO

Sequence cautioni

The sequence BAA92381.1 differs from that shown. Reason: Frameshift at positions 512 and 526.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040669
Natural varianti91 – 911S → L.1 Publication
Corresponds to variant rs55842804 [ dbSNP | Ensembl ].
VAR_040670
Natural varianti324 – 3241A → V.1 Publication
Corresponds to variant rs558614 [ dbSNP | Ensembl ].
VAR_019789
Natural varianti363 – 3631G → S.
Corresponds to variant rs2770928 [ dbSNP | Ensembl ].
VAR_047077
Natural varianti799 – 7991I → V.1 Publication
Corresponds to variant rs35368391 [ dbSNP | Ensembl ].
VAR_040671
Natural varianti1014 – 10141A → G.1 Publication
Corresponds to variant rs45523141 [ dbSNP | Ensembl ].
VAR_040672
Natural varianti1025 – 10251L → P.1 Publication
Corresponds to variant rs56116059 [ dbSNP | Ensembl ].
VAR_040673

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 613RQQ → SSK in BAA92381. 1 Publication
Sequence conflicti436 – 4361T → S in BAA92381. 1 Publication
Sequence conflicti711 – 7111A → V in AAF80561. 1 Publication
Sequence conflicti868 – 8681C → S in BAA92381. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF207547 mRNA. Translation: AAF80561.1.
AK314235 mRNA. Translation: BAG36905.1.
AL161613, AL356285 Genomic DNA. Translation: CAH71526.1.
AL356285, AL161613 Genomic DNA. Translation: CAI15861.1.
CH471075 Genomic DNA. Translation: EAX08286.1.
AB028019 mRNA. Translation: BAA92381.1. Frameshift.
CCDSiCCDS9294.1.
RefSeqiNP_055387.2. NM_014572.2.
XP_005266399.1. XM_005266342.1.
UniGeneiHs.78960.

Genome annotation databases

EnsembliENST00000382592; ENSP00000372035; ENSG00000150457.
ENST00000542899; ENSP00000441817; ENSG00000150457.
GeneIDi26524.
KEGGihsa:26524.
UCSCiuc001unr.4. human.

Polymorphism databases

DMDMi212276441.

Keywords - Coding sequence diversityi

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
AF207547 mRNA. Translation: AAF80561.1 .
AK314235 mRNA. Translation: BAG36905.1 .
AL161613 , AL356285 Genomic DNA. Translation: CAH71526.1 .
AL356285 , AL161613 Genomic DNA. Translation: CAI15861.1 .
CH471075 Genomic DNA. Translation: EAX08286.1 .
AB028019 mRNA. Translation: BAA92381.1 . Frameshift.
CCDSi CCDS9294.1.
RefSeqi NP_055387.2. NM_014572.2.
XP_005266399.1. XM_005266342.1.
UniGenei Hs.78960.

3D structure databases

ProteinModelPortali Q9NRM7.
SMRi Q9NRM7. Positions 92-139, 640-1042.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117727. 144 interactions.
IntActi Q9NRM7. 8 interactions.
MINTi MINT-1772003.
STRINGi 9606.ENSP00000372035.

Chemistry

BindingDBi Q9NRM7.
ChEMBLi CHEMBL5907.
GuidetoPHARMACOLOGYi 1516.

PTM databases

PhosphoSitei Q9NRM7.

Polymorphism databases

DMDMi 212276441.

Proteomic databases

MaxQBi Q9NRM7.
PaxDbi Q9NRM7.
PRIDEi Q9NRM7.

Protocols and materials databases

DNASUi 26524.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382592 ; ENSP00000372035 ; ENSG00000150457 .
ENST00000542899 ; ENSP00000441817 ; ENSG00000150457 .
GeneIDi 26524.
KEGGi hsa:26524.
UCSCi uc001unr.4. human.

Organism-specific databases

CTDi 26524.
GeneCardsi GC13M021547.
H-InvDB HIX0022357.
HGNCi HGNC:6515. LATS2.
HPAi HPA039191.
MIMi 604861. gene.
neXtProti NX_Q9NRM7.
PharmGKBi PA30302.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000040002.
HOVERGENi HBG052311.
InParanoidi Q9NRM7.
KOi K08791.
OMAi GSHIRQD.
OrthoDBi EOG7BZVS1.
PhylomeDBi Q9NRM7.
TreeFami TF351549.

Enzyme and pathway databases

Reactomei REACT_118607. Signaling by Hippo.
SignaLinki Q9NRM7.

Miscellaneous databases

ChiTaRSi LATS2. human.
GeneWikii LATS2.
GenomeRNAii 26524.
NextBioi 48850.
PROi Q9NRM7.
SOURCEi Search...

Gene expression databases

Bgeei Q9NRM7.
CleanExi HS_LATS2.
Genevestigatori Q9NRM7.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR028742. LATS2.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view ]
PANTHERi PTHR24356:SF149. PTHR24356:SF149. 1 hit.
Pfami PF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 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.
PS00107. PROTEIN_KINASE_ATP. 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. "Molecular cloning of a novel human protein kinase, kpm, that is homologous to warts/lats, a Drosophila tumor suppressor."
    Hori T., Takaori-Kondo A., Kamikubo Y., Uchiyama T.
    Oncogene 19:3101-3109(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-697.
    Tissue: Myeloid.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Structure, expression, and chromosome mapping of LATS2, a mammalian homologue of the Drosophila tumor suppressor gene lats/warts."
    Yabuta N., Fujii T., Copeland N.G., Gilbert D.J., Jenkins N.A., Nishiguchi H., Endo Y., Toji S., Tanaka H., Nishimune Y., Nojima H.
    Genomics 63:263-270(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-1088, TISSUE SPECIFICITY, VARIANT VAL-324.
    Tissue: Testis.
  6. "Lats2, a putative tumor suppressor, inhibits G1/S transition."
    Li Y., Pei J., Xia H., Ke H., Wang H., Tao W.
    Oncogene 22:4398-4405(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-697 AND SER-872.
  7. "The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase."
    Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S., Tamai K., Nojima H.
    Genes Cells 9:383-397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKA, MUTAGENESIS OF SER-83, PHOSPHORYLATION AT SER-83.
  8. Cited for: FUNCTION, INTERACTION WITH AR.
  9. "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.
  10. "LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis."
    Abe Y., Ohsugi M., Haraguchi K., Fujimoto J., Yamamoto T.
    FEBS Lett. 580:782-788(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AJUBA.
  11. "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.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. "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.
  15. "Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation."
    Zhang K., Rodriguez-Aznar E., Yabuta N., Owen R.J., Mingot J.M., Nojima H., Nieto M.A., Longmore G.D.
    EMBO J. 31:29-43(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNAI1, PHOSPHORYLATION AT THR-1041.
  16. "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] GLU-40; LEU-91; VAL-799; GLY-1014 AND PRO-1025.

Entry informationi

Entry nameiLATS2_HUMAN
AccessioniPrimary (citable) accession number: Q9NRM7
Secondary accession number(s): B1AM47, Q9P2X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: November 4, 2008
Last modified: September 3, 2014
This is version 131 of the entry and version 2 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 13
    Human chromosome 13: 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

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