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Q7TSJ6

- LATS2_MOUSE

UniProt

Q7TSJ6 - LATS2_MOUSE

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Protein

Serine/threonine-protein kinase LATS2

Gene
Lats2
Organism
Mus musculus (Mouse)
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 By similarity.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Magnesium By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei655 – 6551ATP By similarityBy similarity
Active sitei749 – 7491Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi632 – 6409ATP By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein localization Source: MGI
  2. G1/S transition of mitotic cell cycle Source: UniProtKB
  3. hippo signaling Source: MGI
  4. hormone-mediated signaling pathway Source: UniProtKB
  5. intracellular signal transduction Source: UniProtKB
  6. keratinocyte differentiation Source: MGI
  7. mitotic nuclear division Source: UniProtKB-KW
  8. negative regulation of canonical Wnt signaling pathway Source: MGI
  9. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  10. protein phosphorylation Source: UniProtKB
  11. regulation of organ growth Source: MGI
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_196537. Signaling by Hippo.

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
Gene namesi
Name:Lats2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1354386. Lats2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasm. Cytoplasmcytoskeletonspindle pole. Nucleus By similarity
Note: Colocalizes with AURKA at the centrosomes during interphase, early prophase and cytokinesis By similarity. Migrates to the spindle poles during mitosis, and to the midbody during cytokinesis. Translocates to the nucleus upon mitotic stress by nocodazole treatment By similarity.1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10421042Serine/threonine-protein kinase LATS2PRO_0000086235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphoserine; by AURKA By similarityBy similarity
Modified residuei267 – 2671Phosphothreonine By similarity
Modified residuei999 – 9991Phosphothreonine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7TSJ6.
PRIDEiQ7TSJ6.

PTM databases

PhosphoSiteiQ7TSJ6.

Expressioni

Tissue specificityi

Expressed at high levels in ovary and testis and at lower levels in all other tissues examined.1 Publication

Gene expression databases

ArrayExpressiQ7TSJ6.
BgeeiQ7TSJ6.
CleanExiMM_LATS2.
GenevestigatoriQ7TSJ6.

Interactioni

Subunit structurei

Interacts with and is phosphorylated by AURKA. Binds to AR By similarity. 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 By similarity. Interacts with LIMD1, WTIP and AJUBA By similarity. Interacts with SNAI1 By similarity.

Protein-protein interaction databases

IntActiQ7TSJ6. 124 interactions.
MINTiMINT-4100233.

Structurei

Secondary structure

1
1042
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi100 – 11011
Helixi113 – 12311
Helixi128 – 13811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COSNMR-A98-138[»]
ProteinModelPortaliQ7TSJ6.
SMRiQ7TSJ6. Positions 91-138, 600-961.

Miscellaneous databases

EvolutionaryTraceiQ7TSJ6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 13842UBAAdd
BLAST
Domaini626 – 931306Protein kinaseAdd
BLAST
Domaini932 – 101079AGC-kinase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi472 – 4754PPxY motif

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117422.
HOGENOMiHOG000040002.
HOVERGENiHBG052311.
InParanoidiQ7TSJ6.
KOiK08791.
OMAiGSHIRQD.
PhylomeDBiQ7TSJ6.
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.

Q7TSJ6-1 [UniParc]FASTAAdd to Basket

« Hide

MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KASTQGLLVG PNSDTSLDAK     50
VLGSKDASRQ QQMRATPKFG PYQKALREIR YSLLPFANES GTSAAAEVNR 100
QMLQELVNAG CDQEMAGRAL KQTGSRSIEA ALEYISKMGY LDPRNEQIVR 150
VIKQTSPGKG LAPTPVTRRP SFEGTGEALP SYHQLGGANY EGPAALEEMP 200
RQYLDFLFPG AGAGTHGAQA HQHPPKGYST AVEPSAHFPG THYGRGHLLS 250
EQPGYGVQRS SSFQNKTPPD AYSSMAKAQG GPPASLTFPA HAGLYTASHH 300
KPAATPPGAH PLHVLGTRGP TFTGESSAQA VLAPSRNSLN ADLYELGSTV 350
PWSAAPLARR DSLQKQGLEA SRPHVAFRAG PSRTNSFNNP QPEPSLPAPN 400
TVTAVTAAHI LHPVKSVRVL RPEPQTAVGP SHPAWVAAPT APATESLETK 450
EGSAGPHPLD VDYGGSERRC PPPPYPKHLL LPSKSEQYSV DLDSLCTSVQ 500
QSLRGGTEQD RSDKSHKGAK GDKAGRDKKQ IQTSPVPVRK NSRDEEKRES 550
RIKSYSPYAF KFFMEQHVEN VIKTYQQKVS RRLQLEQEMA KAGLCEAEQE 600
QMRKILYQKE SNYNRLKRAK MDKSMFVKIK TLGIGAFGEV CLACKLDTHA 650
LYAMKTLRKK DVLNRNQVAH VKAERDILAE ADNEWVVKLY YSFQDKDSLY 700
FVMDYIPGGD MMSLLIRMEV FPEHLARFYI AELTLAIESV HKMGFIHRDI 750
KPDNILIDLD GHIKLTDFGL CTGFRWTHNS KYYQKGNHMR QDSMEPGDLW 800
DDVSNCRCGD RLKTLEQRAQ KQHQRCLAHS LVGTPNYIAP EVLLRKGYTQ 850
LCDWWSVGVI LFEMLVGQPP FLAPTPTETQ LKVINWESTL HIPTQVRLSA 900
EARDLITKLC CAADCRLGRD GADDLKAHPF FNTIDFSRDI RKQPAPYVPT 950
ISHPMDTSNF DPVDEESPWH EASGESAKAW DTLASPSSKH PEHAFYEFTF 1000
RRFFDDNGYP FRCPKPSEPA ESADPGDADL EGAAEGCQPV YV 1042
Length:1,042
Mass (Da):115,472
Last modified:October 1, 2003 - v1
Checksum:i7E0E73A73DB954C0
GO

Sequence cautioni

The sequence BAC26704.1 differs from that shown. Reason: Frameshift at positions 970, 1025 and 1037.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841Q → R in BAA92380. 1 Publication
Sequence conflicti279 – 2791Q → R in BAC26704. 1 Publication
Sequence conflicti549 – 5491E → K in BAC26704. 1 Publication
Sequence conflicti589 – 5891M → V in BAA92380. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023958 mRNA. Translation: BAA92380.1.
AK029966 mRNA. Translation: BAC26704.1. Frameshift.
BC053028 mRNA. Translation: AAH53028.1.
CCDSiCCDS27158.1.
RefSeqiNP_056586.2. NM_015771.2.
UniGeneiMm.347899.

Genome annotation databases

EnsembliENSMUST00000022531; ENSMUSP00000022531; ENSMUSG00000021959.
GeneIDi50523.
KEGGimmu:50523.
UCSCiuc007udk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023958 mRNA. Translation: BAA92380.1 .
AK029966 mRNA. Translation: BAC26704.1 . Frameshift.
BC053028 mRNA. Translation: AAH53028.1 .
CCDSi CCDS27158.1.
RefSeqi NP_056586.2. NM_015771.2.
UniGenei Mm.347899.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2COS NMR - A 98-138 [» ]
ProteinModelPortali Q7TSJ6.
SMRi Q7TSJ6. Positions 91-138, 600-961.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q7TSJ6. 124 interactions.
MINTi MINT-4100233.

PTM databases

PhosphoSitei Q7TSJ6.

Proteomic databases

PaxDbi Q7TSJ6.
PRIDEi Q7TSJ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022531 ; ENSMUSP00000022531 ; ENSMUSG00000021959 .
GeneIDi 50523.
KEGGi mmu:50523.
UCSCi uc007udk.1. mouse.

Organism-specific databases

CTDi 26524.
MGIi MGI:1354386. Lats2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117422.
HOGENOMi HOG000040002.
HOVERGENi HBG052311.
InParanoidi Q7TSJ6.
KOi K08791.
OMAi GSHIRQD.
PhylomeDBi Q7TSJ6.
TreeFami TF351549.

Enzyme and pathway databases

Reactomei REACT_196537. Signaling by Hippo.

Miscellaneous databases

ChiTaRSi LATS2. mouse.
EvolutionaryTracei Q7TSJ6.
NextBioi 307518.
PROi Q7TSJ6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7TSJ6.
Bgeei Q7TSJ6.
CleanExi MM_LATS2.
Genevestigatori Q7TSJ6.

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. "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], TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  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].
    Strain: C57BL/6.
    Tissue: Brain.
  4. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Solution structure of RSGI RUH-038, a UBA domain from mouse LATS2 (large tumor suppressor homolog 2)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 98-138.

Entry informationi

Entry nameiLATS2_MOUSE
AccessioniPrimary (citable) accession number: Q7TSJ6
Secondary accession number(s): Q8CDJ4, Q9JMI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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