dbPTM

LATS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LATS1_HUMAN
UniProt AC	O95835
Protein Name	Serine/threonine-protein kinase LATS1
Gene Name	LATS1 {ECO:0000312\|EMBL:AAD16882.1}
Organism	Homo sapiens (Human).
Sequence Length	1130
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis.
Protein Description	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. Plays a role in mammary gland epithelial cells differentiation, both through the Hippo signaling pathway and the intracellular estrogen receptor signaling pathway by promoting the degradation of ESR1. [PubMed: 28068668]
Protein Sequence	MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKFGTHHKALQEIRNSLLPFANETNSSRSTSEVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSYQDPRREQMAAAAARPINASMKPGNVQQSVNRKQSWKGSKESLVPQRHGPPLGESVAYHSESPNSQTDVGRPLSGSGISAFVQAHPSNGQRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEPNSQTKRYSGNMEYVISRISPVPPGAWQEGYPPPPLNTSPMNPPNQGQRGISSVPVGRQPIIMQSSSKFNFPSGRPGMQNGTGQTDFMIHQNVVPAGTVNRQPPPPYPLTAANGQSPSALQTGGSAAPSSYTNGSIPQSMMVPNRNSHNMELYNISVPGLQTNWPQSSSAPAQSSPSSGHEIPTWQPNIPVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQSASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFFDDNGYPYNYPKPIEYEYINSQGSEQQSDEDDQNTGSEIKNRDLVYV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	YRQMRPKTFPASNYT CCCCCCCCCCCCCCC	37.22	22617229
21	Phosphorylation	RPKTFPASNYTVSSR CCCCCCCCCCCCCHH	30.52	23186163
23	Phosphorylation	KTFPASNYTVSSRQM CCCCCCCCCCCHHHH	13.16	23403867
26	Phosphorylation	PASNYTVSSRQMLQE CCCCCCCCHHHHHHH	16.41	-
27	Phosphorylation	ASNYTVSSRQMLQEI CCCCCCCHHHHHHHH	23.38	-
37	Phosphorylation	MLQEIRESLRNLSKP HHHHHHHHHHHCCCH	23.84	24719451
42	Phosphorylation	RESLRNLSKPSDAAK HHHHHHCCCHHHHHH	46.17	21712546
76	Ubiquitination	PKFGTHHKALQEIRN CCCCCHHHHHHHHHH	43.09	29967540
84	Phosphorylation	ALQEIRNSLLPFANE HHHHHHHHHHHHCCC	22.79	27050516
92	Phosphorylation	LLPFANETNSSRSTS HHHHCCCCCCCCCCC	39.96	26546556
94	Phosphorylation	PFANETNSSRSTSEV HHCCCCCCCCCCCCC	34.25	26546556
139	Phosphorylation	EAAIEFISKMSYQDP HHHHHHHHHCCCCCH	27.85	28270605
142	Phosphorylation	IEFISKMSYQDPRRE HHHHHHCCCCCHHHH	24.31	28270605
143	Phosphorylation	EFISKMSYQDPRREQ HHHHHCCCCCHHHHH	17.28	28270605
171	Phosphorylation	KPGNVQQSVNRKQSW CCCCHHHHHCCCCCC	12.31	24260401
177	Phosphorylation	QSVNRKQSWKGSKES HHHCCCCCCCCCHHH	33.52	20363803
181	Phosphorylation	RKQSWKGSKESLVPQ CCCCCCCCHHHCCCC	29.53	23927012
184	Phosphorylation	SWKGSKESLVPQRHG CCCCCHHHCCCCCCC	38.10	27794612
197	Phosphorylation	HGPPLGESVAYHSES CCCCCCCCEEECCCC	15.39	27174698
200	Phosphorylation	PLGESVAYHSESPNS CCCCCEEECCCCCCC	12.06	27174698
202	Phosphorylation	GESVAYHSESPNSQT CCCEEECCCCCCCCC	27.39	27174698
204	Phosphorylation	SVAYHSESPNSQTDV CEEECCCCCCCCCCC	32.18	25159151
207	Phosphorylation	YHSESPNSQTDVGRP ECCCCCCCCCCCCCC	37.53	27174698
209	Phosphorylation	SESPNSQTDVGRPLS CCCCCCCCCCCCCCC	32.26	27174698
216	Phosphorylation	TDVGRPLSGSGISAF CCCCCCCCCCCCHHE	33.33	27174698
218	Phosphorylation	VGRPLSGSGISAFVQ CCCCCCCCCCHHEEE	29.58	27174698
221	Phosphorylation	PLSGSGISAFVQAHP CCCCCCCHHEEEECC	21.12	27174698
229	Phosphorylation	AFVQAHPSNGQRVNP HEEEECCCCCCCCCC	43.66	27174698
243	Methylation	PPPPPQVRSVTPPPP CCCCCCCCCCCCCCC	21.84	115383981
244	Phosphorylation	PPPPQVRSVTPPPPP CCCCCCCCCCCCCCC	31.33	30266825
246	Phosphorylation	PPQVRSVTPPPPPRG CCCCCCCCCCCCCCC	31.18	30266825
252	Methylation	VTPPPPPRGQTPPPR CCCCCCCCCCCCCCC	56.47	115481877
255	Phosphorylation	PPPPRGQTPPPRGTT CCCCCCCCCCCCCCC	40.35	23911959
259	Methylation	RGQTPPPRGTTPPPP CCCCCCCCCCCCCCC	61.95	115383989
261	Phosphorylation	QTPPPRGTTPPPPSW CCCCCCCCCCCCCCC	37.09	18691976
262	Phosphorylation	TPPPRGTTPPPPSWE CCCCCCCCCCCCCCC	36.30	25850435
267	Phosphorylation	GTTPPPPSWEPNSQT CCCCCCCCCCCCCCC	50.25	23312004
275	Methylation	WEPNSQTKRYSGNME CCCCCCCCCCCCCCE	41.52	115481885
277	Phosphorylation	PNSQTKRYSGNMEYV CCCCCCCCCCCCEEE	23.61	23401153
278	Phosphorylation	NSQTKRYSGNMEYVI CCCCCCCCCCCEEEE	27.94	23401153
283	Phosphorylation	RYSGNMEYVISRISP CCCCCCEEEEEEEEC	7.72	23401153
286	Phosphorylation	GNMEYVISRISPVPP CCCEEEEEEEECCCC	17.33	23401153
289	Phosphorylation	EYVISRISPVPPGAW EEEEEEEECCCCCCC	20.80	26074081
321	Phosphorylation	NQGQRGISSVPVGRQ CCCCCCCCCCCCCCC	28.27	28555341
322	Phosphorylation	QGQRGISSVPVGRQP CCCCCCCCCCCCCCC	28.64	29457462
334	Phosphorylation	RQPIIMQSSSKFNFP CCCEEEECCCCCCCC	21.14	17322306
335	Phosphorylation	QPIIMQSSSKFNFPS CCEEEECCCCCCCCC	22.21	17322306
336	Phosphorylation	PIIMQSSSKFNFPSG CEEEECCCCCCCCCC	46.65	-
376	Phosphorylation	NRQPPPPYPLTAANG CCCCCCCCCCCCCCC	19.35	24043423
379	Phosphorylation	PPPPYPLTAANGQSP CCCCCCCCCCCCCCC	21.15	24043423
385	Phosphorylation	LTAANGQSPSALQTG CCCCCCCCCCHHCCC	23.40	24043423
387	Phosphorylation	AANGQSPSALQTGGS CCCCCCCCHHCCCCC	47.02	24043423
391	Phosphorylation	QSPSALQTGGSAAPS CCCCHHCCCCCCCCC	44.34	24043423
394	Phosphorylation	SALQTGGSAAPSSYT CHHCCCCCCCCCCCC	23.70	19369195
398	Phosphorylation	TGGSAAPSSYTNGSI CCCCCCCCCCCCCCC	31.11	24043423
399	Phosphorylation	GGSAAPSSYTNGSIP CCCCCCCCCCCCCCC	34.61	24043423
400	Phosphorylation	GSAAPSSYTNGSIPQ CCCCCCCCCCCCCCH	14.46	24043423
401	Phosphorylation	SAAPSSYTNGSIPQS CCCCCCCCCCCCCHH	34.74	24043423
404	Phosphorylation	PSSYTNGSIPQSMMV CCCCCCCCCCHHHCC	32.92	24043423
408	Phosphorylation	TNGSIPQSMMVPNRN CCCCCCHHHCCCCCC	11.95	24043423
462	Phosphorylation	QPNIPVRSNSFNNPL CCCCCCCCCCCCCCC	36.74	30266825
464	Phosphorylation	NIPVRSNSFNNPLGN CCCCCCCCCCCCCCC	30.51	25159151
490	Phosphorylation	ATTVTAITPAPIQQP CCEEEEEECCCCCCC	15.78	12372621
573	Phosphorylation	QNPSVPPYESISKPS CCCCCCCCCCCCCCC	19.08	29978859
575	Phosphorylation	PSVPPYESISKPSKE CCCCCCCCCCCCCCC	26.73	25627689
577	Phosphorylation	VPPYESISKPSKEDQ CCCCCCCCCCCCCCC	48.03	29978859
580	Phosphorylation	YESISKPSKEDQPSL CCCCCCCCCCCCCCC	53.03	-
596	Phosphorylation	KEDESEKSYENVDSG CCCCCHHHHCCCCCC	33.36	28796482
597	Phosphorylation	EDESEKSYENVDSGD CCCCHHHHCCCCCCC	23.69	28796482
611	Phosphorylation	DKEKKQITTSPITVR CHHHCCCCCCCEEEE	20.80	22167270
612	Phosphorylation	KEKKQITTSPITVRK HHHCCCCCCCEEEEC	33.85	29255136
613	Phosphorylation	EKKQITTSPITVRKN HHCCCCCCCEEEECC	12.98	29255136
616	Phosphorylation	QITTSPITVRKNKKD CCCCCCEEEECCCCH	20.03	23927012
633	Phosphorylation	RRESRIQSYSPQAFK HHHHHHHHHCHHHHH	25.80	15688006
635	Phosphorylation	ESRIQSYSPQAFKFF HHHHHHHCHHHHHHH	18.78	25159151
662	Ubiquitination	QQRLHRKKQLENEMM HHHHHHHHHHHHHHH	61.13	29967540
674	Phosphorylation	EMMRVGLSQDAQDQM HHHHHCCCHHHHHHH	21.78	17525332
688	Ubiquitination	MRKMLCQKESNYIRL HHHHHHHHHHHHHHH	63.21	29967540
728	Ubiquitination	LARKVDTKALYATKT HHCCCCHHHHHHCCC	31.75	29967540
734	Ubiquitination	TKALYATKTLRKKDV HHHHHHCCCHHHHHH	37.07	29967540
751	Sumoylation	RNQVAHVKAERDILA HCHHHHHHHHHHHHH	34.36	-
792	Phosphorylation	IPGGDMMSLLIRMGI CCCCCHHHHHHHCCC	17.24	-
830	Sumoylation	GFIHRDIKPDNILID CCCCCCCCCCCEEEC	51.08	-
859	Phosphorylation	GFRWTHDSKYYQSGD CCCCCCCCCCCCCCC	18.23	29496907
860	Ubiquitination	FRWTHDSKYYQSGDH CCCCCCCCCCCCCCC	54.77	-
861	Phosphorylation	RWTHDSKYYQSGDHP CCCCCCCCCCCCCCC	15.64	29496907
864	Phosphorylation	HDSKYYQSGDHPRQD CCCCCCCCCCCCCCC	30.02	-
872	Phosphorylation	GDHPRQDSMDFSNEW CCCCCCCCCCCCCCC	16.35	15688006
876	Phosphorylation	RQDSMDFSNEWGDPS CCCCCCCCCCCCCHH	29.58	24043423
883	Phosphorylation	SNEWGDPSSCRCGDR CCCCCCHHHCCCCCC	46.97	24043423
884	Phosphorylation	NEWGDPSSCRCGDRL CCCCCHHHCCCCCCC	15.80	24043423
909	Phosphorylation	HQRCLAHSLVGTPNY HHHHHHHHCCCCCCC	21.10	25850435
913	Phosphorylation	LAHSLVGTPNYIAPE HHHHCCCCCCCCCHH	10.81	25850435
967	Phosphorylation	MKVINWQTSLHIPPQ HEEEEEECCCCCCCC	25.52	15688006
976	Ubiquitination	LHIPPQAKLSPEASD CCCCCCCCCCHHHHH	44.22	29967540
982	Phosphorylation	AKLSPEASDLIIKLC CCCCHHHHHHHHHHH	31.15	-
1005	Ubiquitination	KNGADEIKAHPFFKT CCCCHHHHCCCCCEE	38.30	29967540
1012	Phosphorylation	KAHPFFKTIDFSSDL HCCCCCEECCCCHHH	22.18	15688006
1029	Ubiquitination	QSASYIPKITHPTDT HCHHCCCCCCCCCCC	51.16	29967540
1046	Ubiquitination	FDPVDPDKLWSDDNE CCCCCHHHCCCCCCC	58.19	29967540
1049	Phosphorylation	VDPDKLWSDDNEEEN CCHHHCCCCCCCCCC	45.59	15688006
1060	Phosphorylation	EEENVNDTLNGWYKN CCCCCHHHHCHHHHC	19.54	15688006
1076	Phosphorylation	KHPEHAFYEFTFRRF CCCCCEEEEEEEHHH	15.77	23917254
1079	Phosphorylation	EHAFYEFTFRRFFDD CCEEEEEEEHHHCCC	12.32	10673337
1099	Phosphorylation	NYPKPIEYEYINSQG CCCCCEEEEEECCCC	18.10	20873877
1101	Phosphorylation	PKPIEYEYINSQGSE CCCEEEEEECCCCCC	12.42	29978859
1104	Phosphorylation	IEYEYINSQGSEQQS EEEEEECCCCCCCCC	26.76	20873877
1107	Phosphorylation	EYINSQGSEQQSDED EEECCCCCCCCCCCC	25.29	20873877
1111	Phosphorylation	SQGSEQQSDEDDQNT CCCCCCCCCCCCCCC	42.53	25159151
1118	Phosphorylation	SDEDDQNTGSEIKNR CCCCCCCCCHHHCCC	36.13	28270605
1120	Phosphorylation	EDDQNTGSEIKNRDL CCCCCCCHHHCCCCC	33.82	28270605
1129	Phosphorylation	IKNRDLVYV------ HCCCCCEEC------	14.03	23917254

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
464	S	Phosphorylation	Kinase	NUAK1	O60285	Uniprot
464	S	Phosphorylation	Kinase	NUAK2	Q9H093	Uniprot
490	T	Phosphorylation	Kinase	CDK1	P06493	PSP
613	S	Phosphorylation	Kinase	CDK1	P06493	PSP
674	S	Phosphorylation	Kinase	LATS1	O95835	PSP
872	S	Phosphorylation	Kinase	STK3	Q13188	GPS
909	S	Phosphorylation	Kinase	LATS1	O95835	PSP
909	S	Phosphorylation	Kinase	STK3	Q13188	GPS
967	T	Phosphorylation	Kinase	STK3	Q13188	GPS
1012	T	Phosphorylation	Kinase	STK3	Q13188	GPS
1049	S	Phosphorylation	Kinase	LATS1	O95835	PSP
1060	T	Phosphorylation	Kinase	STK3	Q13188	GPS
1079	T	Phosphorylation	Kinase	HGK	O95819	PSP
1079	T	Phosphorylation	Kinase	STK3	Q13188	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:21383157
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:24107629
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1	Q9H0M0	PMID:23573293
-	K	Ubiquitination	E3 ubiquitin ligase	DCAF1	Q9Y4B6	PMID:25026211

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
464	S	Phosphorylation	18669648
Phosphorylation at Ser-464 by NUAK1 and NUAK2 leads to decreased protein level and is required to regulate cellular senescence and cellular ploidy.
909	S	Phosphorylation	15688006
Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079, which results in its activation.
1079	T	Phosphorylation	15688006
Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079, which results in its activation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of LATS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK1_HUMAN	CDK1	physical	9988268
ITCH_HUMAN	ITCH	physical	21212414
KIBRA_HUMAN	WWC1	physical	21233212
MAST2_HUMAN	MAST2	physical	22195963
LIMK1_HUMAN	LIMK1	physical	15220930
YAP1_HUMAN	YAP1	physical	18413746
ITCH_HUMAN	ITCH	physical	21383157
YAP1_HUMAN	YAP1	physical	21383157
AURKB_HUMAN	AURKB	physical	21822051
HTRA2_HUMAN	HTRA2	physical	17130845
ASPP1_HUMAN	PPP1R13B	physical	21041411
YAP1_HUMAN	YAP1	physical	21041411
MOB1A_HUMAN	MOB1A	physical	16061636
YAP1_HUMAN	YAP1	physical	20841485
HTRA2_HUMAN	HTRA2	physical	16007220
XIAP_HUMAN	XIAP	physical	16007220
YAP1_HUMAN	YAP1	physical	18158288
MOB1A_HUMAN	MOB1A	physical	20624913
RAF1_HUMAN	RAF1	physical	17889669
YAP1_HUMAN	YAP1	physical	17889669
YAP1_HUMAN	YAP1	physical	18640976
MOB1A_HUMAN	MOB1A	physical	16674920
MOB1B_HUMAN	MOB1B	physical	16674920
NPHP4_HUMAN	NPHP4	physical	21555462
WWTR1_HUMAN	WWTR1	physical	21555462
A4_HUMAN	APP	physical	21832049
FOXL2_HUMAN	FOXL2	physical	20407010
NUAK1_HUMAN	NUAK1	physical	19927127
YAP1_HUMAN	YAP1	physical	22863277
MOB1B_HUMAN	MOB1B	physical	18328708
PP1RB_HUMAN	PPP1R11	physical	22641346
PP6R3_HUMAN	PPP6R3	physical	22641346
PPB1_HUMAN	ALPP	physical	22641346
MYPT1_HUMAN	PPP1R12A	physical	22641346
PTEN_HUMAN	PTEN	physical	22641346
YAP1_HUMAN	YAP1	physical	22641346
HTRA2_HUMAN	HTRA2	physical	22641346
PLK1_HUMAN	PLK1	physical	22641346
PP1G_HUMAN	PPP1CC	physical	22641346
4EBP1_HUMAN	EIF4EBP1	physical	22641346
AMOT_HUMAN	AMOT	physical	24255178
AMOL1_HUMAN	AMOTL1	physical	24255178
ASSY_HUMAN	ASS1	physical	24255178
CP131_HUMAN	CEP131	physical	24255178
CP110_HUMAN	CCP110	physical	24255178
CE152_HUMAN	CEP152	physical	24255178
CING_HUMAN	CGN	physical	24255178
CNTRB_HUMAN	CNTROB	physical	24255178
DJC11_HUMAN	DNAJC11	physical	24255178
INADL_HUMAN	INADL	physical	24255178
K1549_HUMAN	KIAA1549	physical	24255178
KIRR1_HUMAN	KIRREL	physical	24255178
LATS2_HUMAN	LATS2	physical	24255178
LIMD1_HUMAN	LIMD1	physical	24255178
LZTS2_HUMAN	LZTS2	physical	24255178
MAGI1_HUMAN	MAGI1	physical	24255178
MPP5_HUMAN	MPP5	physical	24255178
OFD1_HUMAN	OFD1	physical	24255178
PARD3_HUMAN	PARD3	physical	24255178
PKP4_HUMAN	PKP4	physical	24255178
PTN13_HUMAN	PTPN13	physical	24255178
PTN14_HUMAN	PTPN14	physical	24255178
RAB35_HUMAN	RAB35	physical	24255178
SDCG3_HUMAN	SDCCAG3	physical	24255178
SC16A_HUMAN	SEC16A	physical	24255178
SI1L2_HUMAN	SIPA1L2	physical	24255178
ZO2_HUMAN	TJP2	physical	24255178
AMOT_HUMAN	AMOT	physical	24101513
HS90B_HUMAN	HSP90AB1	physical	20841485
LDOC1_HUMAN	LDOC1	physical	25416956
TFP11_HUMAN	TFIP11	physical	25416956
MOAP1_HUMAN	MOAP1	physical	25416956
CEP76_HUMAN	CEP76	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
FSD2_HUMAN	FSD2	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
WWTR1_HUMAN	WWTR1	physical	20412773
YAP1_HUMAN	YAP1	physical	24107629
TAZ_HUMAN	TAZ	physical	24107629
ITCH_HUMAN	ITCH	physical	24107629
NEDD4_HUMAN	NEDD4	physical	24107629
WWP1_HUMAN	WWP1	physical	24107629
WWOX_HUMAN	WWOX	physical	24107629
SMUF1_HUMAN	SMURF1	physical	24107629
SMUF2_HUMAN	SMURF2	physical	24107629
CAV1_HUMAN	CAV1	physical	24107629
PABP2_HUMAN	PABPN1	physical	24107629
MAGI3_HUMAN	MAGI3	physical	24107629
KIBRA_HUMAN	WWC1	physical	25023289
PTN14_HUMAN	PTPN14	physical	25023289
MERL_HUMAN	NF2	physical	26045165
LIMD1_HUMAN	LIMD1	physical	20303269
AJUBA_HUMAN	AJUBA	physical	20303269
WTIP_HUMAN	WTIP	physical	20303269
MERL_HUMAN	NF2	physical	24012335
CDK2_HUMAN	CDK2	physical	25218637
CDK1_HUMAN	CDK1	physical	25218637
LIMD1_HUMAN	LIMD1	physical	25127217
CDC26_HUMAN	CDC26	physical	25723520
PP1A_HUMAN	PPP1CA	physical	26116754
WWTR1_HUMAN	WWTR1	physical	26116754
PARD3_HUMAN	PARD3	physical	26116754
KIF23_MOUSE	Kif23	physical	25786116
YAP1_HUMAN	YAP1	physical	27847303
WWTR1_HUMAN	WWTR1	physical	27847303
TFIP8_HUMAN	TNFAIP8	physical	28152516
CUL4A_HUMAN	CUL4A	physical	28420424
USP9X_HUMAN	USP9X	physical	28720576
YAP1_HUMAN	YAP1	physical	28754671
LATS1_HUMAN	LATS1	physical	28754671
SRC_HUMAN	SRC	physical	28754671

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LATS1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Regulation of ploidy and senescence by the AMPK-related kinaseNUAK1."; 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). Cited for: FUNCTION, PHOSPHORYLATION AT SER-464, AND MUTAGENESIS OF SER-464.	19927127 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-246; THR-261;SER-462; SER-464; THR-612 AND SER-613, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; THR-246 ANDSER-464, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-278 ANDSER-464, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-464 ANDSER-613, AND MASS SPECTROMETRY.	18691976 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND MASSSPECTROMETRY.	17525332 [Abstract]
"The Ste20-like kinase Mst2 activates the human large tumor suppressorkinase Lats1."; Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A.,Nigg E.A., Sillje H.H.W.; Oncogene 24:2076-2086(2005). Cited for: PHOSPHORYLATION AT SER-909 AND THR-1079.	15688006 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-277, AND MASSSPECTROMETRY.	17053785 [Abstract]

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