Q9NRM7 (LATS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LATS2
Synonyms:	KPM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1088 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton › centrosome. Cytoplasm. Cytoplasm › cytoskeleton › spindle pole. Nucleus. Note: Co-localizes 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Disease	Tumor suppressor
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from direct assay Ref.6. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular protein localization Inferred from electronic annotation. Source: Compara hippo signaling cascade Inferred from direct assay PubMed 20412773. Source: BHF-UCL hormone-mediated signaling pathway Inferred from direct assay Ref.8. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay Ref.1. Source: UniProtKB keratinocyte differentiation Inferred from electronic annotation. Source: Compara mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of canonical Wnt receptor 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 regulation of organ growth Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol 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_function	ATP 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

With	Entry	#Exp.	IntAct	Notes
MOB1A	Q9H8S9	2	EBI-3506895,EBI-748229
MOB1B	Q7L9L4	2	EBI-3506895,EBI-2558745

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1088	1088	Serine/threonine-protein kinase LATS2		PRO_0000086234
Regions
	Domain	98 – 139	42	UBA
	Domain	668 – 973	306	Protein kinase
	Domain	974 – 1052	79	AGC-kinase C-terminal
	Nucleotide binding	674 – 782	109	ATP By similarity UniProtKB P22612
	Motif	515 – 518	4	PPxY motif
Sites
	Active site	791	1	Proton acceptor By similarity UniProtKB P22612
	Binding site	697	1	ATP Ref.1
Amino acid modifications
	Modified residue	83	1	Phosphoserine; by AURKA Ref.7
	Modified residue	279	1	Phosphothreonine Ref.12
	Modified residue	1041	1	Phosphothreonine Ref.15
Natural variations
	Natural variant	40	1	G → E in a lung adenocarcinoma sample; somatic mutation. Ref.16		VAR_040669
	Natural variant	91	1	S → L. Ref.16 Corresponds to variant rs55842804 [ dbSNP | Ensembl ].		VAR_040670
	Natural variant	324	1	A → V. Ref.5 Corresponds to variant rs558614 [ dbSNP | Ensembl ].		VAR_019789
	Natural variant	363	1	G → S. Corresponds to variant rs2770928 [ dbSNP | Ensembl ].		VAR_047077
	Natural variant	799	1	I → V. Ref.16 Corresponds to variant rs35368391 [ dbSNP | Ensembl ].		VAR_040671
	Natural variant	1014	1	A → G. Ref.16 Corresponds to variant rs45523141 [ dbSNP | Ensembl ].		VAR_040672
	Natural variant	1025	1	L → P. Ref.16 Corresponds to variant rs56116059 [ dbSNP | Ensembl ].		VAR_040673
Experimental info
	Mutagenesis	83	1	S → C: Fails to localize at the centromere during interphase. Ref.7
	Mutagenesis	83	1	S → E: Fails to localize at the centromere during interphase. Ref.7
	Mutagenesis	697	1	K → A: Loss of kinase activity, autophosphorylation and tumor suppressor activity. Ref.1 Ref.6
	Mutagenesis	872	1	S → A: Loss of tumor suppressor activity. Ref.6
	Sequence conflict	59 – 61	3	RQQ → SSK in BAA92381. Ref.5
	Sequence conflict	436	1	T → S in BAA92381. Ref.5
	Sequence conflict	711	1	A → V in AAF80561. Ref.1
	Sequence conflict	868	1	C → S in BAA92381. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9NRM7 [UniParc]. Last modified November 4, 2008. Version 2. Checksum: 2866F6B75637AD36	FASTA	1,088	120,136
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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.
+	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.
IPI	IPI00016690.
RefSeq	NP_055387.2. NM_014572.2.
UniGene	Hs.78960.
3D structure databases
ProteinModelPortal	Q9NRM7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRM7. 3 interactions.
MINT	MINT-1772003.
STRING	9606.ENSP00000372035.
PTM databases
PhosphoSite	Q9NRM7.
Polymorphism databases
DMDM	212276441.
Proteomic databases
PaxDb	Q9NRM7.
PRIDE	Q9NRM7.
Protocols and materials databases
DNASU	26524.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000382592; ENSP00000372035; ENSG00000150457. ENST00000542899; ENSP00000441817; ENSG00000150457.
GeneID	26524.
KEGG	hsa:26524.
UCSC	uc001unr.4. human.
Organism-specific databases
CTD	26524.
GeneCards	GC13M021547.
H-InvDB	HIX0022357.
HGNC	HGNC:6515. LATS2.
HPA	HPA039191.
MIM	604861. gene.
neXtProt	NX_Q9NRM7.
PharmGKB	PA30302.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000040002.
HOVERGEN	HBG052311.
InParanoid	Q9NRM7.
KO	K08791.
OMA	RPSFEGT.
OrthoDB	EOG498V00.
PhylomeDB	Q9NRM7.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
Bgee	Q9NRM7.
CleanEx	HS_LATS2.
Genevestigator	Q9NRM7.
GermOnline	ENSG00000150457. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_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]
Pfam	PF00069. Pkinase. 2 hits. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF46934. UBA_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
BindingDB	Q9NRM7.
ChEMBL	CHEMBL5907.
ChiTaRS	LATS2. human.
GenomeRNAi	26524.
NextBio	48850.
SOURCE	Search...

Entry information

Entry name

LATS2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.