TSC2_HUMAN - dbPTM
TSC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSC2_HUMAN
UniProt AC P49815
Protein Name Tuberin
Gene Name TSC2
Organism Homo sapiens (Human).
Sequence Length 1807
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. At steady state found in association with membranes.
Protein Description In complex with TSC1, this tumor suppressor inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. [PubMed: 12271141]
Protein Sequence MAKPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKSLRIARPPKQGLNNSPPVKEFKESSAAEAFRCRSISVSEHVVRSRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTVASFSSLYQSSCQGQLHRSVSWADSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESQSFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANMASQVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV
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
3Ubiquitination-----MAKPTSKDSG
-----CCCCCCCCCC
61.77-
7Acetylation-MAKPTSKDSGLKEK
-CCCCCCCCCCHHHH
59.3912433467
7Ubiquitination-MAKPTSKDSGLKEK
-CCCCCCCCCCHHHH
59.39-
12AcetylationTSKDSGLKEKFKILL
CCCCCCHHHHHHHHH
63.4812433485
14UbiquitinationKDSGLKEKFKILLGL
CCCCHHHHHHHHHCC
50.82-
16UbiquitinationSGLKEKFKILLGLGT
CCHHHHHHHHHCCCC
43.44-
20UbiquitinationEKFKILLGLGTPRPN
HHHHHHHCCCCCCCC
20.72-
22UbiquitinationFKILLGLGTPRPNPR
HHHHHCCCCCCCCCC
31.69-
23UbiquitinationKILLGLGTPRPNPRS
HHHHCCCCCCCCCCC
22.59-
23PhosphorylationKILLGLGTPRPNPRS
HHHHCCCCCCCCCCC
22.5922199227
30PhosphorylationTPRPNPRSAEGKQTE
CCCCCCCCCCCCCEE
31.7429514088
34UbiquitinationNPRSAEGKQTEFIIT
CCCCCCCCCEEEEEE
45.62-
57UbiquitinationMECGLNNRIRMIGQI
HHCCCCHHHHHHHHH
19.47-
69AcetylationGQICEVAKTKKFEEH
HHHHHHHCCCCHHHH
67.0830593117
69UbiquitinationGQICEVAKTKKFEEH
HHHHHHHCCCCHHHH
67.08-
71UbiquitinationICEVAKTKKFEEHAV
HHHHHCCCCHHHHHH
55.55-
72UbiquitinationCEVAKTKKFEEHAVE
HHHHCCCCHHHHHHH
64.3421890473
72UbiquitinationCEVAKTKKFEEHAVE
HHHHCCCCHHHHHHH
64.3421890473
72UbiquitinationCEVAKTKKFEEHAVE
HHHHCCCCHHHHHHH
64.3421890473
72UbiquitinationCEVAKTKKFEEHAVE
HHHHCCCCHHHHHHH
64.3421890473
72 (in isoform 1)Ubiquitination-64.3421890473
72 (in isoform 2)Ubiquitination-64.3421890473
72 (in isoform 3)Ubiquitination-64.3421890473
72 (in isoform 4)Ubiquitination-64.3421890473
72 (in isoform 5)Ubiquitination-64.3421890473
79UbiquitinationKFEEHAVEALWKAVA
CHHHHHHHHHHHHHH
38.54-
95UbiquitinationLLQPERPLEARHAVL
HHCCCCCHHHHHHHH
11.43-
106UbiquitinationHAVLALLKAIVQGQG
HHHHHHHHHHHCCCH
36.60-
125UbiquitinationVLRALFFKVIKDYPS
HHHHHHHHHHCCCCC
35.40-
128UbiquitinationALFFKVIKDYPSNED
HHHHHHHCCCCCCHH
54.95-
144UbiquitinationHERLEVFKALTDNGR
HHHHHHHHHHHCCCC
47.8921906983
144 (in isoform 1)Ubiquitination-47.8921890473
144 (in isoform 2)Ubiquitination-47.8921890473
144 (in isoform 3)Ubiquitination-47.8921890473
144 (in isoform 4)Ubiquitination-47.8921890473
147PhosphorylationLEVFKALTDNGRHIT
HHHHHHHHCCCCEEE
32.0729954749
188PhosphorylationVNLVKFNSCYLDEYI
HHHHCCCCCCHHHHH
13.79-
201UbiquitinationYIARMVQMICLLCVR
HHHHHHHHHHHHHHH
1.27-
209UbiquitinationICLLCVRTASSVDIE
HHHHHHHCCCCCCCC
15.53-
250UbiquitinationLCRTINVKELCEPCW
HHCCCCHHHHHHHHH
40.24-
258UbiquitinationELCEPCWKLMRNLLG
HHHHHHHHHHHHHHH
38.84-
311PhosphorylationWGAHRLYSLRNSPTS
HCHHHHHHHHCCCCC
25.9924719451
389UbiquitinationTIVHDLLTTVEELCD
HHHHHHHHHHHHHHH
35.77-
401 (in isoform 6)Ubiquitination-28.9021890473
438UbiquitinationAQSIHPAKDGWIQNL
HCCCCCCCCCHHHHH
62.3121890473
438UbiquitinationAQSIHPAKDGWIQNL
HCCCCCCCCCHHHHH
62.3121890473
438UbiquitinationAQSIHPAKDGWIQNL
HCCCCCCCCCHHHHH
62.3121890473
438 (in isoform 1)Ubiquitination-62.3121890473
438 (in isoform 2)Ubiquitination-62.3121890473
438 (in isoform 3)Ubiquitination-62.3121890473
438 (in isoform 4)Ubiquitination-62.3121890473
438 (in isoform 5)Ubiquitination-62.3121890473
540PhosphorylationKVMARSLSPPPELEE
HHHHHHCCCCCCHHH
36.2922817900
585UbiquitinationLPASHATRVYEMLVS
CCCHHHHHHHHHHHH
29.78-
598PhosphorylationVSHIQLHYKHSYTLP
HHHHHCCCCCCCCCC
20.9923917254
601PhosphorylationIQLHYKHSYTLPIAS
HHCCCCCCCCCCCCC
18.7023917254
602PhosphorylationQLHYKHSYTLPIASS
HCCCCCCCCCCCCCH
16.4120068231
603PhosphorylationLHYKHSYTLPIASSI
CCCCCCCCCCCCCHH
29.1320068231
608PhosphorylationSYTLPIASSIRLQAF
CCCCCCCCHHHHHHH
27.3320068231
609UbiquitinationYTLPIASSIRLQAFD
CCCCCCCHHHHHHHH
11.60-
609PhosphorylationYTLPIASSIRLQAFD
CCCCCCCHHHHHHHH
11.6023917254
634UbiquitinationHRLGLPNKDGVVRFS
HHCCCCCCCCEEEEC
54.65-
634 (in isoform 2)Ubiquitination-54.65-
658UbiquitinationPERGSEKKTSGPLSP
CCCCCCCCCCCCCCC
43.82-
658 (in isoform 2)Ubiquitination-43.82-
659PhosphorylationERGSEKKTSGPLSPP
CCCCCCCCCCCCCCC
50.4028450419
660PhosphorylationRGSEKKTSGPLSPPT
CCCCCCCCCCCCCCC
47.4928450419
664PhosphorylationKKTSGPLSPPTGPPG
CCCCCCCCCCCCCCC
31.7825867546
667PhosphorylationSGPLSPPTGPPGPAP
CCCCCCCCCCCCCCC
66.7528464451
704UbiquitinationLKQESDWKVLKLVLG
HHCCCCHHHHHHHHC
42.55-
733UbiquitinationSPCSVDQLCSALCSM
CCCCHHHHHHHHHHH
1.84-
751MethylationPKTLERLRGAPEGFS
HHHHHHHCCCCCCCC
45.51115919061
760PhosphorylationAPEGFSRTDLHLAVV
CCCCCCCHHHHHHHH
41.5427251275
771PhosphorylationLAVVPVLTALISYHN
HHHHHHHHHHHHHHH
21.4727251275
775PhosphorylationPVLTALISYHNYLDK
HHHHHHHHHHHCCCH
22.6127251275
776PhosphorylationVLTALISYHNYLDKT
HHHHHHHHHHCCCHH
6.2627251275
779PhosphorylationALISYHNYLDKTKQR
HHHHHHHCCCHHCHH
11.7227251275
782UbiquitinationSYHNYLDKTKQREMV
HHHHCCCHHCHHHHH
55.84-
865UbiquitinationRNFAAEQYASVFAIS
HHHCHHHHHHEEEEE
7.73-
877 (in isoform 6)Ubiquitination-32.7621890473
881UbiquitinationPYTNPSKFNQYIVCL
CCCCHHHHHHHHHHH
8.93-
907 (in isoform 7)Phosphorylation-45.5829507054
914UbiquitinationDFVPFITKGLRSNVL
CCHHHHCCCCCCCEE
51.6521890473
914UbiquitinationDFVPFITKGLRSNVL
CCHHHHCCCCCCCEE
51.6521890473
914UbiquitinationDFVPFITKGLRSNVL
CCHHHHCCCCCCCEE
51.6521890473
914 (in isoform 1)Ubiquitination-51.6521890473
914 (in isoform 2)Ubiquitination-51.6521890473
914 (in isoform 3)Ubiquitination-51.6521890473
914 (in isoform 4)Ubiquitination-51.6521890473
914 (in isoform 5)Ubiquitination-51.6521890473
918PhosphorylationFITKGLRSNVLLSFD
HHCCCCCCCEEEECC
36.0123312004
919 (in isoform 6)Phosphorylation-23.2529507054
923PhosphorylationLRSNVLLSFDDTPEK
CCCCEEEECCCCCCC
23.5929396449
924UbiquitinationRSNVLLSFDDTPEKD
CCCEEEECCCCCCCC
11.27-
927PhosphorylationVLLSFDDTPEKDSFR
EEEECCCCCCCCCCC
34.8825159151
930UbiquitinationSFDDTPEKDSFRARS
ECCCCCCCCCCCCCC
60.932190698
930 (in isoform 1)Ubiquitination-60.9321890473
930 (in isoform 2)Ubiquitination-60.9321890473
930 (in isoform 3)Ubiquitination-60.9321890473
930 (in isoform 4)Ubiquitination-60.9321890473
932PhosphorylationDDTPEKDSFRARSTS
CCCCCCCCCCCCCCC
27.9229978859
937PhosphorylationKDSFRARSTSLNERP
CCCCCCCCCCCCCCC
22.7425159151
937 (in isoform 3)Phosphorylation-22.7425627689
937 (in isoform 5)Phosphorylation-22.7425627689
938PhosphorylationDSFRARSTSLNERPK
CCCCCCCCCCCCCCC
31.5129514088
939PhosphorylationSFRARSTSLNERPKS
CCCCCCCCCCCCCCC
30.3725159151
939 (in isoform 3)Phosphorylation-30.3729116813
939 (in isoform 5)Phosphorylation-30.3729116813
946PhosphorylationSLNERPKSLRIARPP
CCCCCCCCCCCCCCC
26.09-
951UbiquitinationPKSLRIARPPKQGLN
CCCCCCCCCCCCCCC
45.76-
954UbiquitinationLRIARPPKQGLNNSP
CCCCCCCCCCCCCCC
60.73-
956 (in isoform 2)Phosphorylation-36.1829507054
960PhosphorylationPKQGLNNSPPVKEFK
CCCCCCCCCCHHHHH
29.5225627689
964UbiquitinationLNNSPPVKEFKESSA
CCCCCCHHHHHHCCH
64.31-
966UbiquitinationNSPPVKEFKESSAAE
CCCCHHHHHHCCHHH
9.85-
967MethylationSPPVKEFKESSAAEA
CCCHHHHHHCCHHHH
58.75115979451
979PhosphorylationAEAFRCRSISVSEHV
HHHHHCCEEEHHHHH
23.8829255136
981PhosphorylationAFRCRSISVSEHVVR
HHHCCEEEHHHHHHH
22.3429255136
983PhosphorylationRCRSISVSEHVVRSR
HCCEEEHHHHHHHHH
18.3929978859
993PhosphorylationVVRSRIQTSLTSASL
HHHHHHHHHHCCCCC
24.2728450419
994PhosphorylationVRSRIQTSLTSASLG
HHHHHHHHHCCCCCC
17.1828450419
996PhosphorylationSRIQTSLTSASLGSA
HHHHHHHCCCCCCCC
23.2428450419
997PhosphorylationRIQTSLTSASLGSAD
HHHHHHCCCCCCCCC
22.5819690332
999PhosphorylationQTSLTSASLGSADEN
HHHHCCCCCCCCCCC
32.7923403867
1002PhosphorylationLTSASLGSADENSVA
HCCCCCCCCCCCHHH
37.5328450419
1007PhosphorylationLGSADENSVAQADDS
CCCCCCCHHHCCCHH
19.4428450419
1014UbiquitinationSVAQADDSLKNLHLE
HHHCCCHHHHHHHHH
41.62-
1014PhosphorylationSVAQADDSLKNLHLE
HHHCCCHHHHHHHHH
41.6227251275
1019UbiquitinationDDSLKNLHLELTETC
CHHHHHHHHHHHHHH
27.01-
1043UbiquitinationSNFTAVPKRSPVGEF
HCCCCCCCCCCCCCE
59.93-
1045PhosphorylationFTAVPKRSPVGEFLL
CCCCCCCCCCCCEEE
30.0225106551
1057PhosphorylationFLLAGGRTKTWLVGN
EEECCCCEEEEEECC
35.7820068231
1058UbiquitinationLLAGGRTKTWLVGNK
EECCCCEEEEEECCE
36.02-
1068 (in isoform 2)Ubiquitination-23.67-
1076UbiquitinationVTTSVGTGTRSLLGL
EEEECCCCHHHEECC
17.13-
1079PhosphorylationSVGTGTRSLLGLDSG
ECCCCHHHEECCCCC
27.9923403867
1085PhosphorylationRSLLGLDSGELQSGP
HHEECCCCCCCCCCC
38.9323403867
1088UbiquitinationLGLDSGELQSGPESS
ECCCCCCCCCCCCCC
5.83-
1090PhosphorylationLDSGELQSGPESSSS
CCCCCCCCCCCCCCC
69.7828555341
1094PhosphorylationELQSGPESSSSPGVH
CCCCCCCCCCCCCCC
38.3625159151
1095PhosphorylationLQSGPESSSSPGVHV
CCCCCCCCCCCCCCC
32.9223401153
1096PhosphorylationQSGPESSSSPGVHVR
CCCCCCCCCCCCCCE
50.2429255136
1097PhosphorylationSGPESSSSPGVHVRQ
CCCCCCCCCCCCCEE
27.8529255136
1106UbiquitinationGVHVRQTKEAPAKLE
CCCCEECCCCCHHHH
43.47-
1111UbiquitinationQTKEAPAKLESQAGQ
ECCCCCHHHHHHHCC
52.29-
1121PhosphorylationSQAGQQVSRGARDRV
HHHCCHHHHHHHHHH
22.2129507054
1122MethylationQAGQQVSRGARDRVR
HHCCHHHHHHHHHHH
43.89115919053
1130PhosphorylationGARDRVRSMSGGHGL
HHHHHHHHCCCCCCC
17.9123401153
1132PhosphorylationRDRVRSMSGGHGLRV
HHHHHHCCCCCCCCC
42.7529255136
1147PhosphorylationGALDVPASQFLGSAT
CCEECCHHHHCCCCC
18.5229396449
1150UbiquitinationDVPASQFLGSATSPG
ECCHHHHCCCCCCCC
4.03-
1152PhosphorylationPASQFLGSATSPGPR
CHHHHCCCCCCCCCC
30.4429255136
1154PhosphorylationSQFLGSATSPGPRTA
HHHCCCCCCCCCCCC
36.8329255136
1155PhosphorylationQFLGSATSPGPRTAP
HHCCCCCCCCCCCCC
27.8129255136
1159UbiquitinationSATSPGPRTAPAAKP
CCCCCCCCCCCCCCC
49.81-
1168UbiquitinationAPAAKPEKASAGTRV
CCCCCCCCCCCCCCC
57.05-
1170UbiquitinationAAKPEKASAGTRVPV
CCCCCCCCCCCCCCC
38.00-
1177 (in isoform 7)Phosphorylation-11.9727251275
1179 (in isoform 7)Phosphorylation-63.1828348404
1180UbiquitinationTRVPVQEKTNLAAYV
CCCCCCHHCCHHHHH
26.14-
1181 (in isoform 7)Phosphorylation-34.4128348404
1186PhosphorylationEKTNLAAYVPLLTQG
HHCCHHHHHHHHCCC
9.29-
1189 (in isoform 6)Phosphorylation-6.0427251275
1189 (in isoform 7)Phosphorylation-6.0425159151
1191 (in isoform 6)Phosphorylation-32.4928348404
1193 (in isoform 6)Phosphorylation-21.9628348404
1201 (in isoform 6)Phosphorylation-26.1725159151
1217PhosphorylationMSLENPLSPFSSDIN
EEECCCCCCCCCCCC
25.75-
1225 (in isoform 5)Phosphorylation-33.5127251275
1227 (in isoform 5)Phosphorylation-32.7728348404
1229 (in isoform 5)Phosphorylation-43.6528348404
1237 (in isoform 5)Phosphorylation-13.6625159151
1242UbiquitinationLMAAERFKEHRDTAL
HHHHHHHHHHHCCHH
59.85-
1250PhosphorylationEHRDTALYKSLSVPA
HHHCCHHHHHCCCCC
8.96-
1251UbiquitinationHRDTALYKSLSVPAA
HHCCHHHHHCCCCCC
45.85-
1252PhosphorylationRDTALYKSLSVPAAS
HCCHHHHHCCCCCCC
16.6030631047
1254PhosphorylationTALYKSLSVPAASTA
CHHHHHCCCCCCCCC
32.9025159151
1259PhosphorylationSLSVPAASTAKPPPL
HCCCCCCCCCCCCCC
30.8820363803
1260PhosphorylationLSVPAASTAKPPPLP
CCCCCCCCCCCCCCC
33.6920068231
1262UbiquitinationVPAASTAKPPPLPRS
CCCCCCCCCCCCCCC
59.13-
1269PhosphorylationKPPPLPRSNTVASFS
CCCCCCCCCCCCHHH
34.6127251275
1269 (in isoform 4)Phosphorylation-34.6127251275
1271PhosphorylationPPLPRSNTVASFSSL
CCCCCCCCCCHHHHH
20.7828857561
1271 (in isoform 4)Phosphorylation-20.7828348404
1273 (in isoform 4)Phosphorylation-11.6528348404
1274PhosphorylationPRSNTVASFSSLYQS
CCCCCCCHHHHHHHH
22.7118669648
1281 (in isoform 4)Phosphorylation-21.3725159151
1290PhosphorylationCQGQLHRSVSWADSA
CCCCCCCCCCHHCEE
15.1223401153
1304PhosphorylationAVVMEEGSPGEVPVL
EEEECCCCCCCCCEE
32.7724275569
1330PhosphorylationALGMDRRTDAYSRSS
HHCCCCCCCCCCCCC
26.3529083192
1333PhosphorylationMDRRTDAYSRSSSVS
CCCCCCCCCCCCCCC
13.8727642862
1334PhosphorylationDRRTDAYSRSSSVSS
CCCCCCCCCCCCCCC
27.6630576142
1336PhosphorylationRTDAYSRSSSVSSQE
CCCCCCCCCCCCCHH
22.4826699800
1337PhosphorylationTDAYSRSSSVSSQEE
CCCCCCCCCCCCHHH
33.3827794612
1338PhosphorylationDAYSRSSSVSSQEEK
CCCCCCCCCCCHHHH
27.5427794612
1340PhosphorylationYSRSSSVSSQEEKSL
CCCCCCCCCHHHHHH
28.4030576142
1341PhosphorylationSRSSSVSSQEEKSLH
CCCCCCCCHHHHHHC
39.1823911959
1346PhosphorylationVSSQEEKSLHAEELV
CCCHHHHHHCHHHHH
28.7729255136
1355MethylationHAEELVGRGIPIERV
CHHHHHCCCCCCEEE
32.18115919057
1364PhosphorylationIPIERVVSSEGGRPS
CCCEEEECCCCCCCC
21.5827273156
1365PhosphorylationPIERVVSSEGGRPSV
CCEEEECCCCCCCCE
28.7521712546
1371PhosphorylationSSEGGRPSVDLSFQP
CCCCCCCCEECEECC
27.2325159151
1375PhosphorylationGRPSVDLSFQPSQPL
CCCCEECEECCCCCC
19.8525159151
1379PhosphorylationVDLSFQPSQPLSKSS
EECEECCCCCCCCCC
33.3826074081
1383PhosphorylationFQPSQPLSKSSSSPE
ECCCCCCCCCCCCHH
36.8630576142
1385PhosphorylationPSQPLSKSSSSPELQ
CCCCCCCCCCCHHHH
31.8823927012
1386PhosphorylationSQPLSKSSSSPELQT
CCCCCCCCCCHHHHH
38.2725159151
1387PhosphorylationQPLSKSSSSPELQTL
CCCCCCCCCHHHHHH
57.9323927012
1388PhosphorylationPLSKSSSSPELQTLQ
CCCCCCCCHHHHHHH
25.0925159151
1393PhosphorylationSSSPELQTLQDILGD
CCCHHHHHHHHHHCC
38.7230278072
1411PhosphorylationKADVGRLSPEVKARS
CCCHHCCCHHHHHHC
20.0429255136
1418PhosphorylationSPEVKARSQSGTLDG
CHHHHHHCCCCCCCC
33.2930266825
1420PhosphorylationEVKARSQSGTLDGES
HHHHHCCCCCCCCCC
34.6823927012
1422PhosphorylationKARSQSGTLDGESAA
HHHCCCCCCCCCCCC
27.2430266825
1427PhosphorylationSGTLDGESAAWSASG
CCCCCCCCCCCCCCC
28.9023927012
1431PhosphorylationDGESAAWSASGEDSR
CCCCCCCCCCCCCCC
14.0823403867
1433PhosphorylationESAAWSASGEDSRGQ
CCCCCCCCCCCCCCC
36.8827486199
1437PhosphorylationWSASGEDSRGQPEGP
CCCCCCCCCCCCCCC
33.7326074081
1447PhosphorylationQPEGPLPSSSPRSPS
CCCCCCCCCCCCCCC
51.6523401153
1448PhosphorylationPEGPLPSSSPRSPSG
CCCCCCCCCCCCCCC
42.2825159151
1449PhosphorylationEGPLPSSSPRSPSGL
CCCCCCCCCCCCCCC
28.7725159151
1452PhosphorylationLPSSSPRSPSGLRPR
CCCCCCCCCCCCCCC
27.1425159151
1454PhosphorylationSSSPRSPSGLRPRGY
CCCCCCCCCCCCCCE
52.2730266825
1461PhosphorylationSGLRPRGYTISDSAP
CCCCCCCEECCCCCC
11.3729255136
1462PhosphorylationGLRPRGYTISDSAPS
CCCCCCEECCCCCCC
19.4819664994
1464PhosphorylationRPRGYTISDSAPSRR
CCCCEECCCCCCCCC
20.0823403867
1466PhosphorylationRGYTISDSAPSRRGK
CCEECCCCCCCCCCC
34.9823403867
1469PhosphorylationTISDSAPSRRGKRVE
ECCCCCCCCCCCCCH
34.03-
1470UbiquitinationISDSAPSRRGKRVER
CCCCCCCCCCCCCHH
50.76-
1539PhosphorylationQLLDQIPSYDTHKIA
HHHHCCCCCCCCEEE
36.9528348404
1542PhosphorylationDQIPSYDTHKIAVLY
HCCCCCCCCEEEEEE
19.4828348404
1543UbiquitinationQIPSYDTHKIAVLYV
CCCCCCCCEEEEEEE
19.34-
1571PhosphorylationNEHGSYRYTEFLTGL
CCCCCHHHHHHHHHC
11.4611290735
1574UbiquitinationGSYRYTEFLTGLGRL
CCHHHHHHHHHCCCE
5.96-
1585UbiquitinationLGRLIELKDCQPDKV
CCCEEECCCCCCCCE
43.60-
1586UbiquitinationGRLIELKDCQPDKVY
CCEEECCCCCCCCEE
49.24-
1624UbiquitinationAVFHIATLMPTKDVD
HHHHHHHHCCCCCCC
2.60-
1647PhosphorylationHLGNDFVSIVYNDSG
CCCCCCEEEEECCCC
13.31-
1650PhosphorylationNDFVSIVYNDSGEDF
CCCEEEEECCCCCCE
16.16-
1653PhosphorylationVSIVYNDSGEDFKLG
EEEEECCCCCCEEEE
40.21-
1658UbiquitinationNDSGEDFKLGTIKGQ
CCCCCCEEEEEEEEC
59.33-
1660UbiquitinationSGEDFKLGTIKGQFN
CCCCEEEEEEEECEE
26.45-
1684PhosphorylationDYECNLVSLQCRKDM
CCCCCEEEEECCCCC
18.85-
1689UbiquitinationLVSLQCRKDMEGLVD
EEEEECCCCCCCCCC
69.88-
1697PhosphorylationDMEGLVDTSVAKIVS
CCCCCCCHHHHHHHC
20.02-
1701UbiquitinationLVDTSVAKIVSDRNL
CCCHHHHHHHCCCCC
41.29-
1704PhosphorylationTSVAKIVSDRNLPFV
HHHHHHHCCCCCHHH
34.03-
1730PhosphorylationSQVHHSRSNPTDIYP
HHCCCCCCCCCCCCC
50.6127251275
1736PhosphorylationRSNPTDIYPSKWIAR
CCCCCCCCCHHHHHH
12.3125147952
1739UbiquitinationPTDIYPSKWIARLRH
CCCCCCHHHHHHHHH
37.81-
1760PhosphorylationRICEEAAYSNPSLPL
HHHHHHHHCCCCCCC
18.9421945579
1761PhosphorylationICEEAAYSNPSLPLV
HHHHHHHCCCCCCCC
37.2221945579
1764PhosphorylationEAAYSNPSLPLVHPP
HHHHCCCCCCCCCCC
47.0421945579
1772PhosphorylationLPLVHPPSHSKAPAQ
CCCCCCCCCCCCCCC
44.8621712546
1774PhosphorylationLVHPPSHSKAPAQTP
CCCCCCCCCCCCCCC
34.5521712546
1775UbiquitinationVHPPSHSKAPAQTPA
CCCCCCCCCCCCCCC
53.63-
1780PhosphorylationHSKAPAQTPAEPTPG
CCCCCCCCCCCCCCC
26.9421945579
1785PhosphorylationAQTPAEPTPGYEVGQ
CCCCCCCCCCCCHHH
22.3521945579
1788PhosphorylationPAEPTPGYEVGQRKR
CCCCCCCCCHHHCHH
14.5121945579
1798PhosphorylationGQRKRLISSVEDFTE
HHCHHHHCCHHHHHH
32.6827273156
1799PhosphorylationQRKRLISSVEDFTEF
HCHHHHCCHHHHHHC
23.6425159151
1804PhosphorylationISSVEDFTEFV----
HCCHHHHHHCC----
40.6123403867

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
664SPhosphorylationKinaseERK-SUBFAMILY-GPS
664SPhosphorylationKinaseMAPK3P27361
GPS
664SPhosphorylationKinaseMAPK1P28482
GPS
932SPhosphorylationKinasePKCDQ05655
PSP
939SPhosphorylationKinaseAKT1P31749
Uniprot
939SPhosphorylationKinasePKB_GROUP-PhosphoELM
939SPhosphorylationKinaseAKT-FAMILY-GPS
939SPhosphorylationKinaseRPS6KA1Q15418
GPS
939SPhosphorylationKinasePKCDQ05655
PSP
939SPhosphorylationKinaseSGK1O00141
PSP
981SPhosphorylationKinaseSGK1O00141
PSP
981SPhosphorylationKinaseAKT1P31749
PSP
1130SPhosphorylationKinaseSGK1O00141
PSP
1132SPhosphorylationKinaseSGK1O00141
PSP
1217SPhosphorylationKinaseCDK6Q00534
PSP
1217SPhosphorylationKinaseCDK4P11802
PSP
1254SPhosphorylationKinaseMAPK2P49137
PhosphoELM
1271TPhosphorylationKinaseAMPKQ9Y478
Uniprot
1330TPhosphorylationKinaseAMPK-FAMILY-GPS
1387SPhosphorylationKinaseAMPKQ9Y478
Uniprot
1387SPhosphorylationKinaseBRSK2Q8IWQ3
PSP
1448SPhosphorylationKinaseAMPK-FAMILY-GPS
1452SPhosphorylationKinaseCDK6Q00534
PSP
1452SPhosphorylationKinaseCDK4P11802
PSP
1462TPhosphorylationKinaseSGK1O00141
PSP
1462TPhosphorylationKinaseRPS6KA1Q15418
GPS
1462TPhosphorylationKinaseAKT-FAMILY-GPS
1462TPhosphorylationKinaseAKT1P31749
Uniprot
1462TPhosphorylationKinasePKB_GROUP-PhosphoELM
1798SPhosphorylationKinaseSGK1O00141
PSP
1798SPhosphorylationKinaseP90RSKQ15418
PSP
1798SPhosphorylationKinaseAKT-FAMILY-GPS
1798SPhosphorylationKinaseRSK-SUBFAMILY-GPS
1798SPhosphorylationKinaseRSK_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:18298802
-KUbiquitinationE3 ubiquitin ligaseFBXW5Q969U6
PMID:18381890
-KUbiquitinationE3 ubiquitin ligaseMYCBP2O75592
PMID:14559897
-KUbiquitinationE3 ubiquitin ligaseHERC1Q15751
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
939SPhosphorylation

12150915
1387SPhosphorylation

14651849
1418SPhosphorylation

15963462
1420SPhosphorylation

15963462
1462TPhosphorylation

12150915
1798SPhosphorylation

15342917

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
69Acetylation61 (8)RQ;P;Lrs45502703
  • Obesity-related traits
23251661

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433Z_HUMANYWHAZphysical
12176984
AKT1_HUMANAKT1physical
12167664
AKT1_HUMANAKT1physical
15342917
CAV1_HUMANCAV1physical
12147258
FOXO1_HUMANFOXO1physical
17077083
GSK3B_HUMANGSK3Bphysical
12511557
AMD_HUMANPAMphysical
14559897
AAPK1_HUMANPRKAA1physical
14651849
FAK1_HUMANPTK2physical
17043358
RAB5A_HUMANRAB5Aphysical
12147258
RAP1A_HUMANRAP1Aphysical
12147258
RHEB_HUMANRHEBphysical
12869586
RHEB_HUMANRHEBphysical
12820960
RHEB_HUMANRHEBphysical
12771962
RHEB_HUMANRHEBphysical
17077083
RHEB_HUMANRHEBphysical
12842888
KS6A1_HUMANRPS6KA1physical
15342917
TSC1_HUMANTSC1physical
12167664
TSC1_HUMANTSC1physical
11741833
TSC1_HUMANTSC1physical
11290735
TSC1_HUMANTSC1physical
9580671
TSC1_HUMANTSC1physical
12176984
TSC1_HUMANTSC1physical
15340059
TSC1_HUMANTSC1physical
12511557
TSC1_HUMANTSC1physical
15851026
TSC1_HUMANTSC1physical
16636147
TSC1_HUMANTSC1physical
17077083
AXIN1_HUMANAXIN1physical
12511557
UBE3A_HUMANUBE3Aphysical
18298802
TSC1_HUMANTSC1physical
17658474
TBCD7_HUMANTBC1D7physical
17658474
1433B_HUMANYWHABphysical
12582162
1433B_HUMANYWHABphysical
12468542
1433B_HUMANYWHABphysical
12364343
1433B_HUMANYWHABphysical
12176984
HERC1_HUMANHERC1physical
16464865
TSC1_HUMANTSC1physical
16464865
ESR1_HUMANESR1physical
15039427
TSC1_HUMANTSC1physical
15851513
SMAD2_HUMANSMAD2physical
15066998
SMAD3_HUMANSMAD3physical
15066998
1433T_HUMANYWHAQphysical
20618440
MDFI_HUMANMDFIphysical
24722188
SPERT_HUMANSPERTphysical
24722188
TSC1_HUMANTSC1physical
20166753
SIR1_HUMANSIRT1physical
20169165
RRAGA_HUMANRRAGAphysical
24529380
RRAGB_HUMANRRAGBphysical
24529380
RRAGC_HUMANRRAGCphysical
24529380
RRAGD_HUMANRRAGDphysical
24529380
CBY1_HUMANCBY1physical
27173435
RUVB2_HUMANRUVBL2physical
28561026
TBCD7_HUMANTBC1D7physical
28561026
TSC1_HUMANTSC1physical
28561026
TSC2_HUMANTSC2physical
28561026
1433G_HUMANYWHAGphysical
28561026
MCE1_HUMANRNGTTgenetic
26350902
CCNT1_HUMANCCNT1genetic
26350902
CD11A_HUMANCDK11Agenetic
26350902

Drug and Disease Associations
Kegg Disease
H00896 Lymphangioleiomyomatosis (LAM)
H00915 Tuberous sclerosis complex (TSC); Bourneville-Pringle disease
OMIM Disease
613254Tuberous sclerosis 2 (TSC2)
606690Lymphangioleiomyomatosis (LAM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TSC2_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-1155; SER-1449; THR-1462AND SER-1798, AND MASS SPECTROMETRY.
"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-1388 AND SER-1420, ANDMASS SPECTROMETRY.
"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-927; SER-981; SER-1132;SER-1155; SER-1334; SER-1337; SER-1338; SER-1341; SER-1411; SER-1420;SER-1449 AND SER-1452, AND MASS SPECTROMETRY.
"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 SER-1155 AND SER-1411, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1097 AND SER-1155, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1411 AND SER-1798, ANDMASS SPECTROMETRY.
"Phosphorylation and binding partner analysis of the TSC1-TSC2complex.";
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J.,Luider T.M.;
Biochem. Biophys. Res. Commun. 333:818-826(2005).
Cited for: PHOSPHORYLATION AT SER-1387; SER-1418 AND SER-1420, MASS SPECTROMETRY,INTERACTION WITH HSPA1; HSPA8 AND TSC1, AND CHARACTERIZATION OFVARIANTS TSC2 TRP-611 AND GLN-611.
"Tumor-promoting phorbol esters and activated Ras inactivate thetuberous sclerosis tumor suppressor complex via p90 ribosomal S6kinase.";
Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J.;
Proc. Natl. Acad. Sci. U.S.A. 101:13489-13494(2004).
Cited for: PHOSPHORYLATION AT SER-1798.
"TSC2 mediates cellular energy response to control cell growth andsurvival.";
Inoki K., Zhu T., Guan K.L.;
Cell 115:577-590(2003).
Cited for: PHOSPHORYLATION AT THR-1330 AND SER-1448, AND MUTAGENESIS OF THR-1330AND SER-1448.
"Identification of the tuberous sclerosis complex-2 tumor suppressorgene product tuberin as a target of the phosphoinositide 3-kinase/aktpathway.";
Manning B.D., Tee A.R., Logsdon M.N., Blenis J., Cantley L.C.;
Mol. Cell 10:151-162(2002).
Cited for: PHOSPHORYLATION AT SER-939 AND THR-1462.

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