Reviewed, UniProtKB/Swiss-Prot Q7TSJ6 (LATS2_MOUSE)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase LATS2
    EC=2.7.11.1
Alternative name(s):
    Large tumor suppressor homolog 2
    Serine/threonine-protein kinase kpm
    Kinase phosphorylated during mitosis protein

Gene names

Name:

Lats2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1042 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Subunit structure	Interacts with and is phosphorylated by STK6. Binds to AR By similarity. Interacts with JUB during mitosis and this complex regulates organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome By similarity.
Subcellular location	Centrosome. Cytoplasm. Note= Co-localizes with STK6 at the centrosomes during interphase, early prophase and cytokinesis. Migrates to the spindle poles during mitosis, and to the midbody during cytokinesis.
Tissue specificity	Expressed at high levels in ovary and testis and at lower levels in all other tissues examined.
Post-translational modification	Autophosphorylated and phosphorylated during M-phase and the G1/S-phase of the cell cycle. Phosphorylated and activated by STK3 By similarity.
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 BAC26704.1 differs from that shown. Reason: Frameshift at positions 970, 1025 and 1037.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Anti-oncogene Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Ref.4 Inferred from direct assay. Source: UniProtKB hormone-mediated signaling Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cyclin-dependent protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	spindle pole Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 1042

1042

Serine/threonine-protein kinase LATS2

Regions

Domain

97 – 138

42

UBA

Domain

626 – 931

306

Protein kinase

Domain

932 – 1010

79

AGC-kinase C-terminal

Nucleotide binding

632 – 640

9

ATP By similarity

Sites

Active site

749

1

Proton acceptor By similarity

Binding site

655

1

ATP By similarity

Amino acid modifications

Modified residue

82

1

Phosphoserine; by STK6 By similarity

Experimental info

Sequence conflict

184

1

Q → R in BAA92380. Ref.1

Sequence conflict

279

1

Q → R in BAC26704. Ref.2

Sequence conflict

549

1

E → K in BAC26704. Ref.2

Sequence conflict

589

1

M → V in BAA92380. Ref.1

Secondary structure

1

.

.

.

.

.

1042

Helix Strand Turn

Details...

Helix

100 – 110

11

Helix

113 – 123

11

Sequences

	Sequence		Length	Mass (Da)
	Q7TSJ6-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 7E0E73A73DB954C0	FASTA	1,042	115,472
	10 20 30 40 50 60 MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KASTQGLLVG PNSDTSLDAK VLGSKDASRQ 70 80 90 100 110 120 QQMRATPKFG PYQKALREIR YSLLPFANES GTSAAAEVNR QMLQELVNAG CDQEMAGRAL 130 140 150 160 170 180 KQTGSRSIEA ALEYISKMGY LDPRNEQIVR VIKQTSPGKG LAPTPVTRRP SFEGTGEALP 190 200 210 220 230 240 SYHQLGGANY EGPAALEEMP RQYLDFLFPG AGAGTHGAQA HQHPPKGYST AVEPSAHFPG 250 260 270 280 290 300 THYGRGHLLS EQPGYGVQRS SSFQNKTPPD AYSSMAKAQG GPPASLTFPA HAGLYTASHH 310 320 330 340 350 360 KPAATPPGAH PLHVLGTRGP TFTGESSAQA VLAPSRNSLN ADLYELGSTV PWSAAPLARR 370 380 390 400 410 420 DSLQKQGLEA SRPHVAFRAG PSRTNSFNNP QPEPSLPAPN TVTAVTAAHI LHPVKSVRVL 430 440 450 460 470 480 RPEPQTAVGP SHPAWVAAPT APATESLETK EGSAGPHPLD VDYGGSERRC PPPPYPKHLL 490 500 510 520 530 540 LPSKSEQYSV DLDSLCTSVQ QSLRGGTEQD RSDKSHKGAK GDKAGRDKKQ IQTSPVPVRK 550 560 570 580 590 600 NSRDEEKRES RIKSYSPYAF KFFMEQHVEN VIKTYQQKVS RRLQLEQEMA KAGLCEAEQE 610 620 630 640 650 660 QMRKILYQKE SNYNRLKRAK MDKSMFVKIK TLGIGAFGEV CLACKLDTHA LYAMKTLRKK 670 680 690 700 710 720 DVLNRNQVAH VKAERDILAE ADNEWVVKLY YSFQDKDSLY FVMDYIPGGD MMSLLIRMEV 730 740 750 760 770 780 FPEHLARFYI AELTLAIESV HKMGFIHRDI KPDNILIDLD GHIKLTDFGL CTGFRWTHNS 790 800 810 820 830 840 KYYQKGNHMR QDSMEPGDLW DDVSNCRCGD RLKTLEQRAQ KQHQRCLAHS LVGTPNYIAP 850 860 870 880 890 900 EVLLRKGYTQ LCDWWSVGVI LFEMLVGQPP FLAPTPTETQ LKVINWESTL HIPTQVRLSA 910 920 930 940 950 960 EARDLITKLC CAADCRLGRD GADDLKAHPF FNTIDFSRDI RKQPAPYVPT ISHPMDTSNF 970 980 990 1000 1010 1020 DPVDEESPWH EASGESAKAW DTLASPSSKH PEHAFYEFTF RRFFDDNGYP FRCPKPSEPA 1030 1040 ESADPGDADL EGAAEGCQPV YV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10673337] [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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"Lats2/Kpm is required for embryonic development, proliferation control and genomic integrity." McPherson J.P., Tamblyn L., Elia A., Migon E., Shehabeldin A., Matysiak-Zablocki E., Lemmers B., Salmena L., Hakem A., Fish J., Kassam F., Squire J., Bruneau B.G., Hande M.P., Hakem R. EMBO J. 23:3677-3688(2004) [PubMed: 15343267] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB023958 mRNA. Translation: BAA92380.1.
AK029966 mRNA. Translation: BAC26704.1. Frameshift.
BC053028 mRNA. Translation: AAH53028.1.

RefSeq

NP_056586.2.

UniGene

Mm.347899

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2COS	NMR	-	A	98-138	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q7TSJ6.

Genome annotation databases

Ensembl

ENSMUSG00000021959. Mus musculus. [Contig view]

GeneID

50523.

KEGG

mmu:50523.

Organism-specific databases

MGI

MGI:1354386. Lats2.

Phylogenomic databases

HOGENOM

Q7TSJ6.

HOVERGEN

Q7TSJ6.

Gene expression databases

ArrayExpress

Q7TSJ6.

CleanEx

MM_LATS2.

GermOnline

ENSMUSG00000021959. Mus musculus.

Family and domain databases

InterPro

IPR000961. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

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]

BLOCKS

Search...

Other Resources

SOURCE

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ProtoNet

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Entry information

Entry name

LATS2_MOUSE

Accession

Primary (citable) accession number: Q7TSJ6
Secondary accession number(s): Q8CDJ4, Q9JMI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	October 1, 2003
Last modified:	July 22, 2008
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)