LATS2_HUMAN - dbPTM
LATS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LATS2_HUMAN
UniProt AC Q9NRM7
Protein Name Serine/threonine-protein kinase LATS2
Gene Name LATS2 {ECO:0000312|EMBL:BAA92381.1}
Organism Homo sapiens (Human).
Sequence Length 1088
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Nucleus. Colocalizes with AURKA at the centrosomes during interphase, early prophase and cytokinesis. Migrates to the spindle poles
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 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..
Protein Sequence MRPKTFPATTYSGNSRQRLQEIREGLKQPSKSSVQGLPAGPNSDTSLDAKVLGSKDATRQQQQMRATPKFGPYQKALREIRYSLLPFANESGTSAAAEVNRQMLQELVNAGCDQEMAGRALKQTGSRSIEAALEYISKMGYLDPRNEQIVRVIKQTSPGKGLMPTPVTRRPSFEGTGDSFASYHQLSGTPYEGPSFGADGPTALEEMPRPYVDYLFPGVGPHGPGHQHQHPPKGYGASVEAAGAHFPLQGAHYGRPHLLVPGEPLGYGVQRSPSFQSKTPPETGGYASLPTKGQGGPPGAGLAFPPPAAGLYVPHPHHKQAGPAAHQLHVLGSRSQVFASDSPPQSLLTPSRNSLNVDLYELGSTSVQQWPAATLARRDSLQKPGLEAPPRAHVAFRPDCPVPSRTNSFNSHQPRPGPPGKAEPSLPAPNTVTAVTAAHILHPVKSVRVLRPEPQTAVGPSHPAWVPAPAPAPAPAPAPAAEGLDAKEEHALALGGAGAFPLDVEYGGPDRRCPPPPYPKHLLLRSKSEQYDLDSLCAGMEQSLRAGPNEPEGGDKSRKSAKGDKGGKDKKQIQTSPVPVRKNSRDEEKRESRIKSYSPYAFKFFMEQHVENVIKTYQQKVNRRLQLEQEMAKAGLCEAEQEQMRKILYQKESNYNRLKRAKMDKSMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDSLYFVMDYIPGGDMMSLLIRMEVFPEHLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKYYQKGSHVRQDSMEPSDLWDDVSNCRCGDRLKTLEQRARKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPAQVKLSPEARDLITKLCCSADHRLGRNGADDLKAHPFFSAIDFSSDIRKQPAPYVPTISHPMDTSNFDPVDEESPWNDASEGSTKAWDTLTSPNNKHPEHAFYEFTFRRFFDDNGYPFRCPKPSGAEASQAESSDLESSDLVDQTEGCQPVYV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MRPKTFPATTYS
---CCCCCCCCCCCC
37.22-
9PhosphorylationRPKTFPATTYSGNSR
CCCCCCCCCCCCCHH
26.89-
10PhosphorylationPKTFPATTYSGNSRQ
CCCCCCCCCCCCHHH
20.14-
11PhosphorylationKTFPATTYSGNSRQR
CCCCCCCCCCCHHHH
15.38-
12PhosphorylationTFPATTYSGNSRQRL
CCCCCCCCCCHHHHH
29.43-
43PhosphorylationGLPAGPNSDTSLDAK
CCCCCCCCCCCHHHH
45.4527251275
45PhosphorylationPAGPNSDTSLDAKVL
CCCCCCCCCHHHHHH
30.8928555341
50UbiquitinationSDTSLDAKVLGSKDA
CCCCHHHHHHCCCHH
37.34-
55UbiquitinationDAKVLGSKDATRQQQ
HHHHHCCCHHHHHHH
49.97-
55AcetylationDAKVLGSKDATRQQQ
HHHHHCCCHHHHHHH
49.9720167786
58PhosphorylationVLGSKDATRQQQQMR
HHCCCHHHHHHHHHH
38.8626546556
67PhosphorylationQQQQMRATPKFGPYQ
HHHHHHCCCCCCHHH
19.3526657352
82PhosphorylationKALREIRYSLLPFAN
HHHHHHHHHHHHCCC
14.8822817900
83PhosphorylationALREIRYSLLPFANE
HHHHHHHHHHHCCCC
17.3710673337
128PhosphorylationLKQTGSRSIEAALEY
HHHHCCHHHHHHHHH
26.8625002506
135PhosphorylationSIEAALEYISKMGYL
HHHHHHHHHHHCCCC
16.0225002506
154UbiquitinationEQIVRVIKQTSPGKG
HHHEEHHHCCCCCCC
44.67-
168O-linked_GlycosylationGLMPTPVTRRPSFEG
CCCCCCCCCCCCCCC
23.3630379171
172PhosphorylationTPVTRRPSFEGTGDS
CCCCCCCCCCCCCCC
33.8322817900
253PhosphorylationFPLQGAHYGRPHLLV
CCCCCCCCCCCEEEC
17.8127642862
272PhosphorylationLGYGVQRSPSFQSKT
CCCCCCCCCCCCCCC
14.0628555341
274PhosphorylationYGVQRSPSFQSKTPP
CCCCCCCCCCCCCCC
36.8430576142
277PhosphorylationQRSPSFQSKTPPETG
CCCCCCCCCCCCCCC
36.1626270265
277O-linked_GlycosylationQRSPSFQSKTPPETG
CCCCCCCCCCCCCCC
36.1630379171
278UbiquitinationRSPSFQSKTPPETGG
CCCCCCCCCCCCCCC
55.02-
279PhosphorylationSPSFQSKTPPETGGY
CCCCCCCCCCCCCCC
49.6918669648
283PhosphorylationQSKTPPETGGYASLP
CCCCCCCCCCCCCCC
41.5026270265
286PhosphorylationTPPETGGYASLPTKG
CCCCCCCCCCCCCCC
8.3825159151
288PhosphorylationPETGGYASLPTKGQG
CCCCCCCCCCCCCCC
26.8026270265
291PhosphorylationGGYASLPTKGQGGPP
CCCCCCCCCCCCCCC
53.7726270265
335PhosphorylationLHVLGSRSQVFASDS
HHCCCCCCCEECCCC
32.1824719451
340O-linked_GlycosylationSRSQVFASDSPPQSL
CCCCEECCCCCCHHH
27.4430379171
340PhosphorylationSRSQVFASDSPPQSL
CCCCEECCCCCCHHH
27.4425850435
342O-linked_GlycosylationSQVFASDSPPQSLLT
CCEECCCCCCHHHCC
35.6630379171
342PhosphorylationSQVFASDSPPQSLLT
CCEECCCCCCHHHCC
35.6625850435
346O-linked_GlycosylationASDSPPQSLLTPSRN
CCCCCCHHHCCCCCC
30.9930379171
346PhosphorylationASDSPPQSLLTPSRN
CCCCCCHHHCCCCCC
30.9925850435
349PhosphorylationSPPQSLLTPSRNSLN
CCCHHHCCCCCCCCC
25.2227251275
351PhosphorylationPQSLLTPSRNSLNVD
CHHHCCCCCCCCCEE
38.5727251275
380PhosphorylationATLARRDSLQKPGLE
HHHHHHHHCCCCCCC
30.7823401153
406PhosphorylationDCPVPSRTNSFNSHQ
CCCCCCCCCCCCCCC
39.2823312004
408PhosphorylationPVPSRTNSFNSHQPR
CCCCCCCCCCCCCCC
25.7825159151
411PhosphorylationSRTNSFNSHQPRPGP
CCCCCCCCCCCCCCC
22.8423312004
431O-linked_GlycosylationPSLPAPNTVTAVTAA
CCCCCCCCEEEEEHH
20.4130379171
433O-linked_GlycosylationLPAPNTVTAVTAAHI
CCCCCCEEEEEHHHH
17.2430379171
436O-linked_GlycosylationPNTVTAVTAAHILHP
CCCEEEEEHHHHHCC
18.7030379171
446PhosphorylationHILHPVKSVRVLRPE
HHHCCCCEEEEECCC
18.5222817900
526PhosphorylationPKHLLLRSKSEQYDL
CCCEECCCCCCCCCH
40.2730576142
528PhosphorylationHLLLRSKSEQYDLDS
CEECCCCCCCCCHHH
31.0425849741
531PhosphorylationLRSKSEQYDLDSLCA
CCCCCCCCCHHHHHH
17.8922115753
535PhosphorylationSEQYDLDSLCAGMEQ
CCCCCHHHHHHHHHH
32.4222115753
543PhosphorylationLCAGMEQSLRAGPNE
HHHHHHHHHHCCCCC
13.4028102081
565AcetylationRKSAKGDKGGKDKKQ
CCCCCCCCCCCCHHH
77.547709875
570AcetylationGDKGGKDKKQIQTSP
CCCCCCCHHHCCCCC
50.4920167786
571AcetylationDKGGKDKKQIQTSPV
CCCCCCHHHCCCCCC
63.8720167786
575PhosphorylationKDKKQIQTSPVPVRK
CCHHHCCCCCCCCCC
36.3130266825
576PhosphorylationDKKQIQTSPVPVRKN
CHHHCCCCCCCCCCC
13.9230266825
598PhosphorylationESRIKSYSPYAFKFF
HHHHHHHCHHHHHHH
20.6521815630
616PhosphorylationHVENVIKTYQQKVNR
HHHHHHHHHHHHHHH
18.5526074081
617PhosphorylationVENVIKTYQQKVNRR
HHHHHHHHHHHHHHH
12.1626074081
620UbiquitinationVIKTYQQKVNRRLQL
HHHHHHHHHHHHHHH
26.42-
651UbiquitinationMRKILYQKESNYNRL
HHHHHHHHHHCHHHH
49.94-
690PhosphorylationCLACKVDTHALYAMK
HHHCCCCHHHHHHHH
16.43-
697UbiquitinationTHALYAMKTLRKKDV
HHHHHHHHHHHHHHC
35.91-
793UbiquitinationGFIHRDIKPDNILID
CCCCCCCCCCCEEEE
51.08-
827UbiquitinationHNSKYYQKGSHVRQD
CCCCCCCCCCCCCCC
46.38-
829PhosphorylationSKYYQKGSHVRQDSM
CCCCCCCCCCCCCCC
26.3312853976
835PhosphorylationGSHVRQDSMEPSDLW
CCCCCCCCCCHHHHH
19.3927251275
839PhosphorylationRQDSMEPSDLWDDVS
CCCCCCHHHHHHHHH
31.8429449344
872PhosphorylationHQRCLAHSLVGTPNY
HHHHHHHHCCCCCCC
21.1025850435
876PhosphorylationLAHSLVGTPNYIAPE
HHHHCCCCCCCCCHH
10.8125850435
939UbiquitinationLHIPAQVKLSPEARD
EECCCEEECCHHHHH
31.03-
950UbiquitinationEARDLITKLCCSADH
HHHHHHHHHHHCCCC
32.31-
968UbiquitinationRNGADDLKAHPFFSA
CCCHHHHHHCCCCCC
52.20-
984UbiquitinationDFSSDIRKQPAPYVP
CCCCCHHHCCCCCCC
62.05-
1024PhosphorylationGSTKAWDTLTSPNNK
CCCCHHHCCCCCCCC
22.6418669648
1026PhosphorylationTKAWDTLTSPNNKHP
CCHHHCCCCCCCCCC
44.2018669648
1027PhosphorylationKAWDTLTSPNNKHPE
CHHHCCCCCCCCCCC
28.8320363803
1038PhosphorylationKHPEHAFYEFTFRRF
CCCCCCEEEEEEHHH
15.7723917254
1041PhosphorylationEHAFYEFTFRRFFDD
CCCEEEEEEHHHCCC
12.3210871863
1051PhosphorylationRFFDDNGYPFRCPKP
HHCCCCCCCCCCCCC
12.88-
1064PhosphorylationKPSGAEASQAESSDL
CCCCCCHHHCCCCCC
22.7922210691
1080PhosphorylationSSDLVDQTEGCQPVY
CCCCCCCCCCCEECC
29.8622210691
1087PhosphorylationTEGCQPVYV------
CCCCEECCC------
13.7122210691

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
83SPhosphorylationKinaseAURAO14965
PSP
172SPhosphorylationKinaseCHEK2O96017
GPS
380SPhosphorylationKinaseAURKAO14965
GPS
380SPhosphorylationKinaseCHEK2O96017
GPS
408SPhosphorylationKinaseCHEK1O14757
GPS
408SPhosphorylationKinaseCHEK2O96017
GPS
446SPhosphorylationKinaseCHEK2O96017
GPS
835SPhosphorylationKinaseCHEK1O14757
GPS
835SPhosphorylationKinaseLATS2Q9NRM7
PSP
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:25438054
-KUbiquitinationE3 ubiquitin ligaseDCAF1Q9Y4B6
PMID:25026211

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LATS2_HUMAN !!

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 LATS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIBRA_HUMANWWC1physical
21233212
LATS1_HUMANLATS1physical
21233212
YAP1_HUMANYAP1physical
19797269
YAP1_HUMANYAP1physical
18413746
ANDR_HUMANARphysical
15131260
AURKB_HUMANAURKBphysical
21822051
ASPP1_HUMANPPP1R13Bphysical
21041411
YAP1_HUMANYAP1physical
21041411
1433G_HUMANYWHAGphysical
21118956
MOB1B_HUMANMOB1Bphysical
19919647
YAP1_HUMANYAP1physical
19919647
STK3_HUMANSTK3physical
19919647
MDM2_HUMANMDM2physical
17015431
SNAI1_HUMANSNAI1physical
21952048
AMOL2_HUMANAMOTL2physical
21832154
YAP1_HUMANYAP1physical
21832154
ASPP1_HUMANPPP1R13Bphysical
21041410
YAP1_HUMANYAP1physical
21041410
AJUBA_HUMANAJUBAphysical
16413547
DYR1A_HUMANDYRK1Aphysical
21498571
AURKA_HUMANAURKAphysical
15147269
MOB1A_HUMANMOB1Aphysical
20624913
YAP1_HUMANYAP1physical
18640976
YAP1_HUMANYAP1physical
22863277
P5CS_HUMANALDH18A1physical
24255178
ALMS1_HUMANALMS1physical
24255178
AMOT_HUMANAMOTphysical
24255178
AMOL1_HUMANAMOTL1physical
24255178
AMOL2_HUMANAMOTL2physical
24255178
APC1_HUMANANAPC1physical
24255178
APC5_HUMANANAPC5physical
24255178
APC_HUMANAPCphysical
24255178
CP131_HUMANCEP131physical
24255178
BAG2_HUMANBAG2physical
24255178
BAG5_HUMANBAG5physical
24255178
CCD77_HUMANCCDC77physical
24255178
CC85C_HUMANCCDC85Cphysical
24255178
DAPLE_HUMANCCDC88Cphysical
24255178
CP110_HUMANCCP110physical
24255178
CENPJ_HUMANCENPJphysical
24255178
CEP72_HUMANCEP72physical
24255178
CEP85_HUMANCEP85physical
24255178
CEP89_HUMANCEP89physical
24255178
CING_HUMANCGNphysical
24255178
CNTRB_HUMANCNTROBphysical
24255178
CPVL_HUMANCPVLphysical
24255178
CSPP1_HUMANCSPP1physical
24255178
CTNB1_HUMANCTNNB1physical
24255178
CUL7_HUMANCUL7physical
24255178
CYLD_HUMANCYLDphysical
24255178
DCAF7_HUMANDCAF7physical
24255178
DNJA3_HUMANDNAJA3physical
24255178
4ET_HUMANEIF4ENIF1physical
24255178
RB6I2_HUMANERC1physical
24255178
AMER1_HUMANAMER1physical
24255178
FXL16_HUMANFBXL16physical
24255178
FUBP3_HUMANFUBP3physical
24255178
GGYF1_HUMANGIGYF1physical
24255178
GRIP1_HUMANGRIP1physical
24255178
IFFO1_HUMANIFFO1physical
24255178
INADL_HUMANINADLphysical
24255178
ECM29_HUMANKIAA0368physical
24255178
JCAD_HUMANKIAA1462physical
24255178
K1549_HUMANKIAA1549physical
24255178
K1671_HUMANKIAA1671physical
24255178
CE295_HUMANCEP295physical
24255178
LATS2_HUMANLATS2physical
24255178
LETM1_HUMANLETM1physical
24255178
LIMD1_HUMANLIMD1physical
24255178
LIN7C_HUMANLIN7Cphysical
24255178
LNX2_HUMANLNX2physical
24255178
LONM_HUMANLONP1physical
24255178
LZTS2_HUMANLZTS2physical
24255178
MAGI1_HUMANMAGI1physical
24255178
TGO1_HUMANMIA3physical
24255178
MIPO1_HUMANMIPOL1physical
24255178
AFAD_HUMANMLLT4physical
24255178
MOB1A_HUMANMOB1Aphysical
24255178
MPDZ_HUMANMPDZphysical
24255178
MPP9_HUMANMPHOSPH9physical
24255178
MPP5_HUMANMPP5physical
24255178
NCK5L_HUMANNCKAP5Lphysical
24255178
NIN_HUMANNINphysical
24255178
NINL_HUMANNINLphysical
24255178
NDK7_HUMANNME7physical
24255178
NOTC1_HUMANNOTCH1physical
24255178
NOTC2_HUMANNOTCH2physical
24255178
NU160_HUMANNUP160physical
24255178
OFD1_HUMANOFD1physical
24255178
PAK4_HUMANPAK4physical
24255178
PARD3_HUMANPARD3physical
24255178
PCM1_HUMANPCM1physical
24255178
PDZ11_HUMANPDZD11physical
24255178
PHLB2_HUMANPHLDB2physical
24255178
PKP4_HUMANPKP4physical
24255178
PKHA1_HUMANPLEKHA1physical
24255178
PKHA5_HUMANPLEKHA5physical
24255178
PKHA7_HUMANPLEKHA7physical
24255178
PKHG1_HUMANPLEKHG1physical
24255178
PLOD1_HUMANPLOD1physical
24255178
PNMA2_HUMANPNMA2physical
24255178
LIPA1_HUMANPPFIA1physical
24255178
LIPB1_HUMANPPFIBP1physical
24255178
ASPP1_HUMANPPP1R13Bphysical
24255178
2AAA_HUMANPPP2R1Aphysical
24255178
2ABA_HUMANPPP2R2Aphysical
24255178
PTN13_HUMANPTPN13physical
24255178
PTN14_HUMANPTPN14physical
24255178
RADIL_HUMANRADILphysical
24255178
NGAP_HUMANRASAL2physical
24255178
RBM15_HUMANRBM15physical
24255178
RCN2_HUMANRCN2physical
24255178
SDCG3_HUMANSDCCAG3physical
24255178
SC16A_HUMANSEC16Aphysical
24255178
SI1L1_HUMANSIPA1L1physical
24255178
SI1L2_HUMANSIPA1L2physical
24255178
SI1L3_HUMANSIPA1L3physical
24255178
SKP1_HUMANSKP1physical
24255178
SKP2_HUMANSKP2physical
24255178
SRBS1_HUMANSORBS1physical
24255178
SPICE_HUMANSPICE1physical
24255178
ADIP_HUMANSSX2IPphysical
24255178
STK3_HUMANSTK3physical
24255178
STK4_HUMANSTK4physical
24255178
STXB4_HUMANSTXBP4physical
24255178
TANC2_HUMANTANC2physical
24255178
TBK1_HUMANTBK1physical
24255178
TBKB1_HUMANTBKBP1physical
24255178
TCHP_HUMANTCHPphysical
24255178
ZO1_HUMANTJP1physical
24255178
ZO2_HUMANTJP2physical
24255178
TNR6B_HUMANTNRC6Bphysical
24255178
ASPP2_HUMANTP53BP2physical
24255178
TRI27_HUMANTRIM27physical
24255178
TRI37_HUMANTRIM37physical
24255178
TBB2A_HUMANTUBB2Aphysical
24255178
TBB6_HUMANTUBB6physical
24255178
UBP54_HUMANUSP54physical
24255178
USP9X_HUMANUSP9Xphysical
24255178
UTRO_HUMANUTRNphysical
24255178
1433F_HUMANYWHAHphysical
24255178
AMOT_HUMANAMOTphysical
24101513
HS90B_HUMANHSP90AB1physical
20841485
TAZ_HUMANTAZphysical
20858893
AMOT_HUMANAMOTphysical
24225952
AMOT_HUMANAMOTphysical
24106267
ABL1_HUMANABL1physical
23852372
CTNB1_HUMANCTNNB1physical
24360964
CDN1A_HUMANCDKN1Aphysical
23886938
LIMD1_HUMANLIMD1physical
20303269
AJUBA_HUMANAJUBAphysical
20303269
WTIP_HUMANWTIPphysical
20303269
STK4_HUMANSTK4physical
26578655
YAP1_HUMANYAP1physical
26578655
RASF1_HUMANRASSF1physical
26578655
LATS2_HUMANLATS2physical
26578655
SIAH1_HUMANSIAH1physical
25587023
WWTR1_HUMANWWTR1physical
25670202
YAP1_HUMANYAP1physical
25670202
LATS2_HUMANLATS2physical
25670202
KIF23_HUMANKIF23physical
25658096
IKKB_HUMANIKBKBphysical
25946971
YAP1_HUMANYAP1physical
26598551
AMOL2_HUMANAMOTL2physical
26598551
ZYX_HUMANZYXphysical
27030211
SIAH2_HUMANSIAH2physical
27030211
KIF23_MOUSEKif23physical
25786116
MOB1A_HUMANMOB1Aphysical
26898830
EZH2_HUMANEZH2physical
27434182
SUZ12_HUMANSUZ12physical
27434182
USP9X_HUMANUSP9Xphysical
28720576
SRC_HUMANSRCphysical
28754671
YAP1_HUMANYAP1physical
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 LATS2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-279 AND SER-380, ANDMASS SPECTROMETRY.
"The centrosomal protein Lats2 is a phosphorylation target of Aurora-Akinase.";
Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S.,Tamai K., Nojima H.;
Genes Cells 9:383-397(2004).
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKA, MUTAGENESIS OF SER-83,AND PHOSPHORYLATION AT SER-83.
"Structure, expression, and chromosome mapping of LATS2, a mammalianhomologue 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).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-1088, TISSUE SPECIFICITY, AND VARIANTVAL-324.

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