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Q9NRM7 (LATS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LATS2
Synonyms:KPM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1088 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 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. Ref.1 Ref.6 Ref.8 Ref.11 Ref.15

Catalytic activity

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

Cofactor

Magnesium. Ref.1

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Subcellular location

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. Ref.6 Ref.7 Ref.15

Tissue specificity

Expressed at high levels in heart and skeletal muscle and at lower levels in all other tissues examined. Ref.1 Ref.5

Post-translational modification

Autophosphorylated and phosphorylated during M-phase and the G1/S-phase of the cell cycle. Phosphorylated and activated by STK3/MST2. Ref.1 Ref.7 Ref.9 Ref.15

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.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   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_processG1/S transition of mitotic cell cycle

Inferred from direct assay Ref.6. Source: UniProtKB

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

hippo signaling

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

hormone-mediated signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

mitosis

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.6. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Non-traceable author statement Ref.5. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10881088Serine/threonine-protein kinase LATS2
PRO_0000086234

Regions

Domain98 – 13942UBA
Domain668 – 973306Protein kinase
Domain974 – 105279AGC-kinase C-terminal
Nucleotide binding674 – 782109ATP By similarity UniProtKB P22612
Motif515 – 5184PPxY motif

Sites

Active site7911Proton acceptor By similarity UniProtKB P22612
Binding site6971ATP Ref.1

Amino acid modifications

Modified residue831Phosphoserine; by AURKA Ref.7
Modified residue2791Phosphothreonine Ref.12
Modified residue10411Phosphothreonine Ref.15

Natural variations

Natural variant401G → E in a lung adenocarcinoma sample; somatic mutation. Ref.16
VAR_040669
Natural variant911S → L. Ref.16
Corresponds to variant rs55842804 [ dbSNP | Ensembl ].
VAR_040670
Natural variant3241A → V. Ref.5
Corresponds to variant rs558614 [ dbSNP | Ensembl ].
VAR_019789
Natural variant3631G → S.
Corresponds to variant rs2770928 [ dbSNP | Ensembl ].
VAR_047077
Natural variant7991I → V. Ref.16
Corresponds to variant rs35368391 [ dbSNP | Ensembl ].
VAR_040671
Natural variant10141A → G. Ref.16
Corresponds to variant rs45523141 [ dbSNP | Ensembl ].
VAR_040672
Natural variant10251L → P. Ref.16
Corresponds to variant rs56116059 [ dbSNP | Ensembl ].
VAR_040673

Experimental info

Mutagenesis831S → C: Fails to localize at the centromere during interphase. Ref.7
Mutagenesis831S → E: Fails to localize at the centromere during interphase. Ref.7
Mutagenesis6971K → A: Loss of kinase activity, autophosphorylation and tumor suppressor activity. Ref.1 Ref.6
Mutagenesis8721S → A: Loss of tumor suppressor activity. Ref.6
Sequence conflict59 – 613RQQ → SSK in BAA92381. Ref.5
Sequence conflict4361T → S in BAA92381. Ref.5
Sequence conflict7111A → V in AAF80561. Ref.1
Sequence conflict8681C → S in BAA92381. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9NRM7 [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: 2866F6B75637AD36

FASTA1,088120,136
        10         20         30         40         50         60 
MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSVQGLPAG PNSDTSLDAK VLGSKDATRQ 

        70         80         90        100        110        120 
QQQMRATPKF GPYQKALREI RYSLLPFANE SGTSAAAEVN RQMLQELVNA GCDQEMAGRA 

       130        140        150        160        170        180 
LKQTGSRSIE AALEYISKMG YLDPRNEQIV RVIKQTSPGK GLMPTPVTRR PSFEGTGDSF 

       190        200        210        220        230        240 
ASYHQLSGTP YEGPSFGADG PTALEEMPRP YVDYLFPGVG PHGPGHQHQH PPKGYGASVE 

       250        260        270        280        290        300 
AAGAHFPLQG AHYGRPHLLV PGEPLGYGVQ RSPSFQSKTP PETGGYASLP TKGQGGPPGA 

       310        320        330        340        350        360 
GLAFPPPAAG LYVPHPHHKQ AGPAAHQLHV LGSRSQVFAS DSPPQSLLTP SRNSLNVDLY 

       370        380        390        400        410        420 
ELGSTSVQQW PAATLARRDS LQKPGLEAPP RAHVAFRPDC PVPSRTNSFN SHQPRPGPPG 

       430        440        450        460        470        480 
KAEPSLPAPN TVTAVTAAHI LHPVKSVRVL RPEPQTAVGP SHPAWVPAPA PAPAPAPAPA 

       490        500        510        520        530        540 
AEGLDAKEEH ALALGGAGAF PLDVEYGGPD RRCPPPPYPK HLLLRSKSEQ YDLDSLCAGM 

       550        560        570        580        590        600 
EQSLRAGPNE PEGGDKSRKS AKGDKGGKDK KQIQTSPVPV RKNSRDEEKR ESRIKSYSPY 

       610        620        630        640        650        660 
AFKFFMEQHV ENVIKTYQQK VNRRLQLEQE MAKAGLCEAE QEQMRKILYQ KESNYNRLKR 

       670        680        690        700        710        720 
AKMDKSMFVK IKTLGIGAFG EVCLACKVDT HALYAMKTLR KKDVLNRNQV AHVKAERDIL 

       730        740        750        760        770        780 
AEADNEWVVK LYYSFQDKDS LYFVMDYIPG GDMMSLLIRM EVFPEHLARF YIAELTLAIE 

       790        800        810        820        830        840 
SVHKMGFIHR DIKPDNILID LDGHIKLTDF GLCTGFRWTH NSKYYQKGSH VRQDSMEPSD 

       850        860        870        880        890        900 
LWDDVSNCRC GDRLKTLEQR ARKQHQRCLA HSLVGTPNYI APEVLLRKGY TQLCDWWSVG 

       910        920        930        940        950        960 
VILFEMLVGQ PPFLAPTPTE TQLKVINWEN TLHIPAQVKL SPEARDLITK LCCSADHRLG 

       970        980        990       1000       1010       1020 
RNGADDLKAH PFFSAIDFSS DIRKQPAPYV PTISHPMDTS NFDPVDEESP WNDASEGSTK 

      1030       1040       1050       1060       1070       1080 
AWDTLTSPNN KHPEHAFYEF TFRRFFDDNG YPFRCPKPSG AEASQAESSD LESSDLVDQT 


EGCQPVYV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The LATS2/KPM tumor suppressor is a negative regulator of the androgen receptor."
Powzaniuk M., McElwee-Witmer S., Vogel R.L., Hayami T., Rutledge S.J., Chen F., Harada S., Schmidt A., Rodan G.A., Freedman L.P., Bai C.
Mol. Endocrinol. 18:2011-2023(2004) [PubMed] [Europe PMC] [Abstract]
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]"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-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. 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] GLU-40; LEU-91; VAL-799; GLY-1014 AND PRO-1025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055387.2. NM_014572.2.
XP_005266399.1. XM_005266342.1.
UniGeneHs.78960.

3D structure databases

ProteinModelPortalQ9NRM7.
SMRQ9NRM7. Positions 92-139, 656-1044.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117727. 143 interactions.
IntActQ9NRM7. 8 interactions.
MINTMINT-1772003.
STRING9606.ENSP00000372035.

Chemistry

BindingDBQ9NRM7.
ChEMBLCHEMBL5907.
GuidetoPHARMACOLOGY1516.

PTM databases

PhosphoSiteQ9NRM7.

Polymorphism databases

DMDM212276441.

Proteomic databases

PaxDbQ9NRM7.
PRIDEQ9NRM7.

Protocols and materials databases

DNASU26524.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000382592; ENSP00000372035; ENSG00000150457.
ENST00000542899; ENSP00000441817; ENSG00000150457.
GeneID26524.
KEGGhsa:26524.
UCSCuc001unr.4. human.

Organism-specific databases

CTD26524.
GeneCardsGC13M021547.
H-InvDBHIX0022357.
HGNCHGNC:6515. LATS2.
HPAHPA039191.
MIM604861. gene.
neXtProtNX_Q9NRM7.
PharmGKBPA30302.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000040002.
HOVERGENHBG052311.
InParanoidQ9NRM7.
KOK08791.
OMAGSHIRQD.
OrthoDBEOG7BZVS1.
PhylomeDBQ9NRM7.
TreeFamTF351549.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9NRM7.

Gene expression databases

BgeeQ9NRM7.
CleanExHS_LATS2.
GenevestigatorQ9NRM7.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
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.
IPR028742. Warts/LATS2.
[Graphical view]
PANTHERPTHR24356:SF2. PTHR24356:SF2. 1 hit.
PfamPF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 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.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
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ChiTaRSLATS2. human.
GeneWikiLATS2.
GenomeRNAi26524.
NextBio48850.
PROQ9NRM7.
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Entry information

Entry nameLATS2_HUMAN
AccessionPrimary (citable) accession number: Q9NRM7
Secondary accession number(s): B1AM47, Q9P2X1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 127 of the entry and version 2 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 13

Human chromosome 13: entries, gene names and cross-references to MIM