WDR59_HUMAN - dbPTM
WDR59_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR59_HUMAN
UniProt AC Q6PJI9
Protein Name GATOR complex protein WDR59 {ECO:0000305}
Gene Name WDR59 {ECO:0000312|HGNC:HGNC:25706}
Organism Homo sapiens (Human).
Sequence Length 974
Subcellular Localization Lysosome membrane .
Protein Description As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. [PubMed: 23723238 It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1]
Protein Sequence MAARWSSENVVVEFRDSQATAMSVDCLGQHAVLSGRRFLYIVNLDAPFEGHRKISRQSKWDIGAVQWNPHDSFAHYFAASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVFEPDLLVTSSVDTYIYIWDIKDTRKPTVALSAVAGASQVKWNKKNANCLATSHDGDVRIWDKRKPSTAVEYLAAHLSKIHGLDWHPDSEHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMVPQLRRENSLLLWNVFDLNTPVHTFVGHDDVVLEFQWRKQKEGSKDYQLVTWSRDQTLRMWRVDSQMQRLCANDILDGVDEFIESISLLPEPEKTLHTEDTDHQHTASHGEEEALKEDPPRNLLEERKSDQLGLPQTLQQEFSLINVQIRNVNVEMDAADRSCTVSVHCSNHRVKMLVKFPAQYPNNAAPSFQFINPTTITSTMKAKLLKILKDTALQKVKRGQSCLEPCLRQLVSCLESFVNQEDSASSNPFALPNSVTPPLPTFARVTTAYGSYQDANIPFPRTSGARFCGAGYLVYFTRPMTMHRAVSPTEPTPRSLSALSAYHTGLIAPMKIRTEAPGNLRLYSGSPTRSEKEQVSISSFYYKERKSRRWKSKREGSDSGNRQIKAAGKVIIQDIACLLPVHKSLGELYILNVNDIQETCQKNAASALLVGRKDLVQVWSLATVATDLCLGPKSDPDLETPWARHPFGRQLLESLLAHYCRLRDVQTLAMLCSVFEAQSRPQGLPNPFGPFPNRSSNLVVSHSRYPSFTSSGSCSSMSDPGLNTGGWNIAGREAEHLSSPWGESSPEELRFGSLTYSDPRERERDQHDKNKRLLDPANTQQFDDFKKCYGEILYRWGLREKRAEVLKFVSCPPDPHKGIEFGVYCSHCRSEVRGTQCAICKGFTFQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHCLLESTF
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
34PhosphorylationLGQHAVLSGRRFLYI
HCCEEEECCCCEEEE		24.5324719451
91UbiquitinationRVDLYKWKDGSGEVG
CEEEEEECCCCCCCC		48.32-
138PhosphorylationYIWDIKDTRKPTVAL
EEEECCCCCCCEEHH		35.2727542207
140UbiquitinationWDIKDTRKPTVALSA
EECCCCCCCEEHHHH		47.32-
142PhosphorylationIKDTRKPTVALSAVA
CCCCCCCEEHHHHHC		22.8024719451
146PhosphorylationRKPTVALSAVAGASQ
CCCEEHHHHHCCCHH		15.8024719451
152PhosphorylationLSAVAGASQVKWNKK
HHHHCCCHHCCCCCC		34.2927542207
155UbiquitinationVAGASQVKWNKKNAN
HCCCHHCCCCCCCCC		37.0929967540
159UbiquitinationSQVKWNKKNANCLAT
HHCCCCCCCCCEEEE		59.0729967540
181PhosphorylationIWDKRKPSTAVEYLA
EECCCCCCHHHHHHH		31.8420873877
182PhosphorylationWDKRKPSTAVEYLAA
ECCCCCCHHHHHHHH		43.1620873877
192PhosphorylationEYLAAHLSKIHGLDW
HHHHHHHHHHCCCCC		21.5017929957
217UbiquitinationSSQDNSVKFWDYRQP
CCCCCCCCCCCCCCC		40.3329967540
226UbiquitinationWDYRQPRKYLNILPC
CCCCCCHHHHEEECC		61.85-
239UbiquitinationPCQVPVWKARYTPFS
CCCCCEEECCCCCCC		24.18-
298UbiquitinationRKQKEGSKDYQLVTW
ECCCCCCCCEEEEEE		71.90-
308 (in isoform 4)Ubiquitination-40.0621906983
348PhosphorylationLLPEPEKTLHTEDTD
CCCCCCCEECCCCCC		23.3129978859
351PhosphorylationEPEKTLHTEDTDHQH
CCCCEECCCCCCCCC		38.3729978859
354PhosphorylationKTLHTEDTDHQHTAS
CEECCCCCCCCCCCC		29.2029978859
359PhosphorylationEDTDHQHTASHGEEE
CCCCCCCCCCCCCHH		24.2428348404
361PhosphorylationTDHQHTASHGEEEAL
CCCCCCCCCCCHHHH		32.9329978859
381 (in isoform 2)Ubiquitination-62.7621906983
381 (in isoform 1)Ubiquitination-62.7621906983
381UbiquitinationRNLLEERKSDQLGLP
CCHHHHHHHHCCCCC		62.7621906983
455 (in isoform 3)Ubiquitination-23.7421906983
466MalonylationAKLLKILKDTALQKV
HHHHHHHHHHHHHHH		57.4126320211
466UbiquitinationAKLLKILKDTALQKV
HHHHHHHHHHHHHHH		57.4129967540
472UbiquitinationLKDTALQKVKRGQSC
HHHHHHHHHHCCCCC		51.0429967540
500PhosphorylationSFVNQEDSASSNPFA
HHCCCCCCCCCCCCC		29.3328348404
502PhosphorylationVNQEDSASSNPFALP
CCCCCCCCCCCCCCC		34.3028348404
503PhosphorylationNQEDSASSNPFALPN
CCCCCCCCCCCCCCC		48.5228348404
511PhosphorylationNPFALPNSVTPPLPT
CCCCCCCCCCCCCCC		25.9828348404
513PhosphorylationFALPNSVTPPLPTFA
CCCCCCCCCCCCCCE		21.0028348404
523PhosphorylationLPTFARVTTAYGSYQ
CCCCEEEEECCCCCC		10.5228857561
524PhosphorylationPTFARVTTAYGSYQD
CCCEEEEECCCCCCC		18.2828857561
558PhosphorylationVYFTRPMTMHRAVSP
EEEECCCCCCCCCCC		16.7124719451
561UbiquitinationTRPMTMHRAVSPTEP
ECCCCCCCCCCCCCC		26.3422505724
564PhosphorylationMTMHRAVSPTEPTPR
CCCCCCCCCCCCCCC		25.7219664994
564 (in isoform 2)Phosphorylation-25.7222210691
566PhosphorylationMHRAVSPTEPTPRSL
CCCCCCCCCCCCCHH		47.2830266825
569PhosphorylationAVSPTEPTPRSLSAL
CCCCCCCCCCHHHHH		25.7130266825
572PhosphorylationPTEPTPRSLSALSAY
CCCCCCCHHHHHHHH		28.0721406692
574PhosphorylationEPTPRSLSALSAYHT
CCCCCHHHHHHHHHC		28.5421406692
575UbiquitinationPTPRSLSALSAYHTG
CCCCHHHHHHHHHCC		15.7222505724
577PhosphorylationPRSLSALSAYHTGLI
CCHHHHHHHHHCCCC		26.8821406692
579PhosphorylationSLSALSAYHTGLIAP
HHHHHHHHHCCCCCC		9.1321406692
581PhosphorylationSALSAYHTGLIAPMK
HHHHHHHCCCCCCEE		22.4721406692
588UbiquitinationTGLIAPMKIRTEAPG
CCCCCCEEEECCCCC		28.1632015554
600PhosphorylationAPGNLRLYSGSPTRS
CCCCEEEEECCCCCC		12.4522199227
601PhosphorylationPGNLRLYSGSPTRSE
CCCEEEEECCCCCCC		37.0728176443
603PhosphorylationNLRLYSGSPTRSEKE
CEEEEECCCCCCCCC		19.7023401153
605PhosphorylationRLYSGSPTRSEKEQV
EEEECCCCCCCCCEE		48.8230266825
607PhosphorylationYSGSPTRSEKEQVSI
EECCCCCCCCCEEEH		56.3422199227
609UbiquitinationGSPTRSEKEQVSISS
CCCCCCCCCEEEHHH		55.48-
611UbiquitinationPTRSEKEQVSISSFY
CCCCCCCEEEHHHHH		45.3822505724
613PhosphorylationRSEKEQVSISSFYYK
CCCCCEEEHHHHHHH		19.2228555341
616PhosphorylationKEQVSISSFYYKERK
CCEEEHHHHHHHHHH		18.6528857561
619PhosphorylationVSISSFYYKERKSRR
EEHHHHHHHHHHCCC		12.3628842319
624PhosphorylationFYYKERKSRRWKSKR
HHHHHHHCCCCCCCC		33.04-
629PhosphorylationRKSRRWKSKREGSDS
HHCCCCCCCCCCCCH		29.95-
642UbiquitinationDSGNRQIKAAGKVII
CHHHHHHHHCCEEEE		24.6829967540
646UbiquitinationRQIKAAGKVIIQDIA
HHHHHCCEEEEEHHH		26.07-
679UbiquitinationDIQETCQKNAASALL
HHHHHHHHHHHHHHH		51.18-
772PhosphorylationFGPFPNRSSNLVVSH
CCCCCCCCCCEEEEC		30.16-
773PhosphorylationGPFPNRSSNLVVSHS
CCCCCCCCCEEEECC		30.8322985185
778PhosphorylationRSSNLVVSHSRYPSF
CCCCEEEECCCCCCC		14.31-
780PhosphorylationSNLVVSHSRYPSFTS
CCEEEECCCCCCCCC		26.4624247654
782PhosphorylationLVVSHSRYPSFTSSG
EEEECCCCCCCCCCC		13.2728857561
784PhosphorylationVSHSRYPSFTSSGSC
EECCCCCCCCCCCCC		32.0228857561
786PhosphorylationHSRYPSFTSSGSCSS
CCCCCCCCCCCCCCC		26.7328857561
787PhosphorylationSRYPSFTSSGSCSSM
CCCCCCCCCCCCCCC		30.5928857561
788PhosphorylationRYPSFTSSGSCSSMS
CCCCCCCCCCCCCCC		31.5027251275
790PhosphorylationPSFTSSGSCSSMSDP
CCCCCCCCCCCCCCC		16.8727251275
792PhosphorylationFTSSGSCSSMSDPGL
CCCCCCCCCCCCCCC		30.6727251275
793PhosphorylationTSSGSCSSMSDPGLN
CCCCCCCCCCCCCCC		27.0027251275
795PhosphorylationSGSCSSMSDPGLNTG
CCCCCCCCCCCCCCC		42.4727251275
815PhosphorylationGREAEHLSSPWGESS
CCCCHHCCCCCCCCC		35.9429978859
816PhosphorylationREAEHLSSPWGESSP
CCCHHCCCCCCCCCH		30.9130266825
821PhosphorylationLSSPWGESSPEELRF
CCCCCCCCCHHHHHH		47.4523401153
822PhosphorylationSSPWGESSPEELRFG
CCCCCCCCHHHHHHC		31.8423401153
830PhosphorylationPEELRFGSLTYSDPR
HHHHHHCCCCCCCHH		18.1530266825
832PhosphorylationELRFGSLTYSDPRER
HHHHCCCCCCCHHHH		23.7630266825
833PhosphorylationLRFGSLTYSDPRERE
HHHCCCCCCCHHHHH		19.1728796482
834PhosphorylationRFGSLTYSDPRERER
HHCCCCCCCHHHHHH		35.5830266825
863UbiquitinationTQQFDDFKKCYGEIL
CCCHHHHHHHHHHHH		49.2627667366
863 (in isoform 1)Ubiquitination-49.2621906983
863AcetylationTQQFDDFKKCYGEIL
CCCHHHHHHHHHHHH		49.2624471169
864UbiquitinationQQFDDFKKCYGEILY
CCHHHHHHHHHHHHH		32.46-
882UbiquitinationLREKRAEVLKFVSCP
CHHHHEEEEEEEECC		7.4122505724
884UbiquitinationEKRAEVLKFVSCPPD
HHHEEEEEEEECCCC		49.2329967540
887PhosphorylationAEVLKFVSCPPDPHK
EEEEEEEECCCCCCC		24.84-
894UbiquitinationSCPPDPHKGIEFGVY
ECCCCCCCCCEEEEE		67.95-
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

Oops, there are no upstream regulatory protein records of WDR59_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR59_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 WDR59_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR5_HUMANWDR5physical
17041588
CAST1_HUMANGATSL3physical
26972053
CAST2_HUMANGATSL2physical
26972053
SESN2_HUMANSESN2physical
26972053
MIO_HUMANMIOSphysical
26972053
GRB10_HUMANGRB10physical
28514442
VIGLN_HUMANHDLBPphysical
28514442
SEC13_HUMANSEC13physical
28514442
NRF1_HUMANNRF1physical
28514442
UEVLD_HUMANUEVLDphysical
28514442
E41L2_HUMANEPB41L2physical
28514442
MOG1_HUMANRANGRFphysical
28514442
TBL1X_HUMANTBL1Xphysical
28514442
CRNN_HUMANCRNNphysical
28514442
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 WDR59_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-830, AND MASSSPECTROMETRY.
"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-564, AND MASSSPECTROMETRY.
"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 SER-821 AND SER-822, ANDMASS SPECTROMETRY.

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