O95835 (LATS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase LATS1
EC=2.7.11.1

Alternative name(s):
Large tumor suppressor homolog 1
WARTS protein kinase
Short name=h-warts

Gene names

Name:	LATS1
Synonyms:	WARTS

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	1130 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 LATS1 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 maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function. Ref.2 Ref.4 Ref.6 Ref.7 Ref.10 Ref.17
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.2 Ref.6
Cofactor	Magnesium. Ref.2 Ref.6
Subunit structure	Complexes with CDK1 in early mitosis. LATS1-associated CDK1 has no mitotic cyclin partner and no apparent kinase activity. Binds phosphorylated ZYX, locating this protein to the mitotic spindle and suggesting a role for actin regulatory proteins during mitosis. Binds to and colocalizes with LIMK1 at the actomyosin contractile ring during cytokinesis. Interacts (via PPxY motif 2) with YAP1 (via WW domains). Interacts with MOB1A and MOB1B. Interacts with LIMD1, WTIP and AJUBA. Ref.1 Ref.4 Ref.7 Ref.10 Ref.15 Ref.16
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Note: Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis. Ref.2
Tissue specificity	Expressed in all adult tissues examined except for lung and kidney. Ref.2
Post-translational modification	Autophosphorylated and phosphorylated during M-phase of the cell cycle. Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079, which results in its activation. Phosphorylation at Ser-464 by NUAK1 and NUAK2 leads to decreased protein level and is required to regulate cellular senescence and cellular ploidy. Ref.1 Ref.2 Ref.6 Ref.8 Ref.17
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing 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	G2/M transition of mitotic cell cycle Inferred from direct assay Ref.6. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW cytoplasmic sequestering of protein Inferred from mutant phenotype PubMed 20412773. Source: BHF-UCL hippo signaling cascade Inferred from direct assay PubMed 20412773. Source: BHF-UCL hormone-mediated signaling pathway Inferred from sequence or structural similarity. 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.1. Source: UniProtKB positive regulation of peptidyl-serine phosphorylation Inferred from direct assay PubMed 20412773. Source: BHF-UCL regulation of actin filament polymerization Inferred from direct assay Ref.7. Source: UniProtKB sister chromatid segregation Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.2. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.2. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK1	P06493	2	EBI-444209,EBI-444308
LIMK1	P53667	5	EBI-444209,EBI-444403
MOB1A	Q9H8S9	2	EBI-444209,EBI-748229
MOB1B	Q7L9L4	2	EBI-444209,EBI-2558745
WWTR1	Q9GZV5	4	EBI-444209,EBI-747743
YAP1	P46937	2	EBI-444209,EBI-1044059
ZYX	Q15942	10	EBI-444209,EBI-444225

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: O95835-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O95835-2)

The sequence of this isoform differs from the canonical sequence as follows:
     672-690: GLSQDAQDQMRKMLCQKES → KPFKMSIFILNHLFAWCLF
     691-1130: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1130	1130	Serine/threonine-protein kinase LATS1		PRO_0000086232
Regions
	Domain	100 – 141	42	UBA
	Domain	705 – 1010	306	Protein kinase
	Domain	1011 – 1090	80	AGC-kinase C-terminal
	Nucleotide binding	711 – 719	9	ATP By similarity UniProtKB P22612
	Region	526 – 655	130	Interaction with YAP1
	Motif	373 – 376	4	PPxY motif 1
	Motif	556 – 559	4	PPxY motif 2
Sites
	Active site	828	1	Proton acceptor By similarity UniProtKB P22612
	Binding site	734	1	ATP Ref.6
Amino acid modifications
	Modified residue	246	1	Phosphothreonine Ref.12
	Modified residue	278	1	Phosphoserine Ref.12
	Modified residue	464	1	Phosphoserine; by NUAK1 and NUAK2 Ref.12 Ref.17
	Modified residue	674	1	Phosphoserine Ref.9
	Modified residue	909	1	Phosphoserine; by STK3/MST2 Ref.8
	Modified residue	1079	1	Phosphothreonine; by STK3/MST2 Ref.8
Natural variations
	Alternative sequence	672 – 690	19	GLSQD…CQKES → KPFKMSIFILNHLFAWCLF in isoform 2.		VSP_051604
	Alternative sequence	691 – 1130	440	Missing in isoform 2.		VSP_051605
	Natural variant	96	1	R → W. Ref.18 Corresponds to variant rs55945045 [ dbSNP | Ensembl ].		VAR_040660
	Natural variant	204	1	S → G. Ref.18 Corresponds to variant rs34793526 [ dbSNP | Ensembl ].		VAR_040661
	Natural variant	237	1	P → Q. Ref.18 Corresponds to variant rs56149740 [ dbSNP | Ensembl ].		VAR_040662
	Natural variant	370	1	R → W. Ref.18 Corresponds to variant rs56348064 [ dbSNP | Ensembl ].		VAR_040663
	Natural variant	531	1	P → S. Ref.18 Corresponds to variant rs55874734 [ dbSNP | Ensembl ].		VAR_040664
	Natural variant	641	1	F → L. Ref.18 Corresponds to variant rs35163691 [ dbSNP | Ensembl ].		VAR_040665
	Natural variant	669	1	M → I in a lung adenocarcinoma sample; somatic mutation. Ref.18		VAR_040666
	Natural variant	806	1	R → P in a lung large cell carcinoma sample; somatic mutation. Ref.18		VAR_040667
	Natural variant	1000	1	G → S. Ref.18 Corresponds to variant rs56412005 [ dbSNP | Ensembl ].		VAR_040668
Experimental info
	Mutagenesis	464	1	S → A: Abolishes phosphorylation by NUAK1 and NUAK2. Ref.17
	Mutagenesis	559	1	Y → F: Loss of interaction with YAP1. Ref.10
	Mutagenesis	734	1	K → A: Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 11CFBCD8FD87DCD8	FASTA	1,130	126,870
	10 20 30 40 50 60 MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA EHNMSKMSTE 70 80 90 100 110 120 DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE VNPQMLQDLQ AAGFDEDMVI 130 140 150 160 170 180 QALQKTNNRS IEAAIEFISK MSYQDPRREQ MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG 190 200 210 220 230 240 SKESLVPQRH GPPLGESVAY HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP 250 260 270 280 290 300 QVRSVTPPPP PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY 310 320 330 340 350 360 PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG TGQTDFMIHQ 370 380 390 400 410 420 NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY TNGSIPQSMM VPNRNSHNME 430 440 450 460 470 480 LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE IPTWQPNIPV RSNSFNNPLG NRASHSANSQ 490 500 510 520 530 540 PSATTVTAIT PAPIQQPVKS MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV 550 560 570 580 590 600 TVMPPVAEAP NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV 610 620 630 640 650 660 DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV LKSHQQRLHR 670 680 690 700 710 720 KKQLENEMMR VGLSQDAQDQ MRKMLCQKES NYIRLKRAKM DKSMFVKIKT LGIGAFGEVC 730 740 750 760 770 780 LARKVDTKAL YATKTLRKKD VLLRNQVAHV KAERDILAEA DNEWVVRLYY SFQDKDNLYF 790 800 810 820 830 840 VMDYIPGGDM MSLLIRMGIF PESLARFYIA ELTCAVESVH KMGFIHRDIK PDNILIDRDG 850 860 870 880 890 900 HIKLTDFGLC TGFRWTHDSK YYQSGDHPRQ DSMDFSNEWG DPSSCRCGDR LKPLERRAAR 910 920 930 940 950 960 QHQRCLAHSL VGTPNYIAPE VLLRTGYTQL CDWWSVGVIL FEMLVGQPPF LAQTPLETQM 970 980 990 1000 1010 1020 KVINWQTSLH IPPQAKLSPE ASDLIIKLCR GPEDRLGKNG ADEIKAHPFF KTIDFSSDLR 1030 1040 1050 1060 1070 1080 QQSASYIPKI THPTDTSNFD PVDPDKLWSD DNEEENVNDT LNGWYKNGKH PEHAFYEFTF 1090 1100 1110 1120 1130 RRFFDDNGYP YNYPKPIEYE YINSQGSEQQ SDEDDQNTGS EIKNRDLVYV
	Isoform 2 [UniParc]. Checksum: 7154097947DF44E8	FASTA	690	76,193
	10 20 30 40 50 60 MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA EHNMSKMSTE 70 80 90 100 110 120 DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE VNPQMLQDLQ AAGFDEDMVI 130 140 150 160 170 180 QALQKTNNRS IEAAIEFISK MSYQDPRREQ MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG 190 200 210 220 230 240 SKESLVPQRH GPPLGESVAY HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP 250 260 270 280 290 300 QVRSVTPPPP PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY 310 320 330 340 350 360 PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG TGQTDFMIHQ 370 380 390 400 410 420 NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY TNGSIPQSMM VPNRNSHNME 430 440 450 460 470 480 LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE IPTWQPNIPV RSNSFNNPLG NRASHSANSQ 490 500 510 520 530 540 PSATTVTAIT PAPIQQPVKS MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV 550 560 570 580 590 600 TVMPPVAEAP NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV 610 620 630 640 650 660 DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV LKSHQQRLHR 670 680 690 KKQLENEMMR VKPFKMSIFI LNHLFAWCLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homologue of the Drosophila melanogaster lats tumour suppressor modulates CDC2 activity." Tao W., Zhang S., Turenchalk G.S., Stewart R.A., St John M.A., Chen W., Xu T. Nat. Genet. 21:177-181(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, INTERACTION WITH CDK1. Tissue: Fetal brain.
[2]	"A human homolog of Drosophila warts tumor suppressor, h-warts, localized to mitotic apparatus and specifically phosphorylated during mitosis." Nishiyama Y., Hirota T., Morisaki T., Hara T., Marumoto T., Iida S., Makino K., Yamamoto H., Hiraoka T., Kitamura N., Saya H. FEBS Lett. 459:159-165(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
[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] (ISOFORM 2). Tissue: Endometrium.
[4]	"Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor." Hirota T., Morisaki T., Nishiyama Y., Marumoto T., Tada K., Hara T., Masuko N., Inagaki M., Hatakeyama K., Saya H. J. Cell Biol. 149:1073-1086(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZYX.
[5]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[6]	"Tumor suppressor WARTS ensures genomic integrity by regulating both mitotic progression and G1 tetraploidy checkpoint function." Iida S., Hirota T., Morisaki T., Marumoto T., Hara T., Kuninaka S., Honda S., Kosai K., Kawasuji M., Pallas D.C., Saya H. Oncogene 23:5266-5274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-734.
[7]	"LATS1 tumour suppressor affects cytokinesis by inhibiting LIMK1." Yang X., Yu K., Hao Y., Li D.-M., Stewart R.A., Insogna K.L., Xu T. Nat. Cell Biol. 6:609-617(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIMK1.
[8]	"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 AT SER-909 AND THR-1079.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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, MUTAGENESIS OF TYR-559.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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-246; SER-278 AND SER-464, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[15]	"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.
[16]	"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.
[17]	"Regulation of ploidy and senescence by the AMPK-related kinase NUAK1." Humbert N., Navaratnam N., Augert A., Da Costa M., Martien S., Wang J., Martinez D., Abbadie C., Carling D., de Launoit Y., Gil J., Bernard D. EMBO J. 29:376-386(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-464, MUTAGENESIS OF SER-464.
[18]	"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] TRP-96; GLY-204; GLN-237; TRP-370; SER-531; LEU-641; ILE-669; PRO-806 AND SER-1000.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF104413 mRNA. Translation: AAD16882.1. AF164041 mRNA. Translation: AAD50272.1. BC002767 mRNA. Translation: AAH02767.1.
IPI	IPI00005858. IPI00470672.
RefSeq	NP_001257448.1. NM_001270519.1. NP_004681.1. NM_004690.3.
UniGene	Hs.549084.
3D structure databases
ProteinModelPortal	O95835.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95835. 9 interactions.
PTM databases
PhosphoSite	O95835.
Proteomic databases
PaxDb	O95835.
PRIDE	O95835.
Protocols and materials databases
DNASU	9113.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253339; ENSP00000253339; ENSG00000131023. ENST00000392273; ENSP00000444678; ENSG00000131023. ENST00000543571; ENSP00000437550; ENSG00000131023.
GeneID	9113.
KEGG	hsa:9113.
UCSC	uc003qmu.1. human. uc003qmw.3. human.
Organism-specific databases
CTD	9113.
GeneCards	GC06M150023.
HGNC	HGNC:6514. LATS1.
HPA	HPA031804.
MIM	603473. gene.
neXtProt	NX_O95835.
PharmGKB	PA30301.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000040002.
HOVERGEN	HBG052311.
InParanoid	O95835.
KO	K08791.
OMA	RYSGNME.
OrthoDB	EOG40GCQ5.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	O95835.
Bgee	O95835.
CleanEx	HS_LATS1.
Genevestigator	O95835.
GermOnline	ENSG00000131023. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. IPR009060. UBA-like. IPR000449. UBA/transl_elong_EF1B_N. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view]
Pfam	PF00069. Pkinase. 2 hits. PF00433. Pkinase_C. 1 hit. PF00627. UBA. 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. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50030. UBA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O95835.
ChEMBL	CHEMBL6167.
GenomeRNAi	9113.
NextBio	34157.
SOURCE	Search...

Entry information

Entry name

LATS1_HUMAN

Accession

Primary (citable) accession number: O95835
Secondary accession number(s): Q6PKD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 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.