TS101_HUMAN - dbPTM
TS101_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TS101_HUMAN
UniProt AC Q99816
Protein Name Tumor susceptibility gene 101 protein
Gene Name TSG101
Organism Homo sapiens (Human).
Sequence Length 390
Subcellular Localization Cytoplasm . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Late endosome membrane
Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Midbody, Midbody ring . Nucleus . Mainly
Protein Description Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan. [PubMed: 22660413 It may also play a role in the extracellular release of microvesicles that differ from the exosomes]
Protein Sequence MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFSRPISASYPPYQATGPPNTSYMPGMPGGISPYPSGYPPNPSGYPGCPYPPGGPYPATTSSQYPSQPPVTTVGPSRDGTISEDTIRASLISAVSDKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARKTAGLSDLY
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
2Acetylation------MAVSESQLK
------CCCCHHHHH
17.3422814378
4Phosphorylation----MAVSESQLKKM
----CCCCHHHHHHH
23.2223401153
6Phosphorylation--MAVSESQLKKMVS
--CCCCHHHHHHHHH
33.0525159151
9AcetylationAVSESQLKKMVSKYK
CCCHHHHHHHHHHHH
31.0525953088
9UbiquitinationAVSESQLKKMVSKYK
CCCHHHHHHHHHHHH
31.0533845483
14AcetylationQLKKMVSKYKYRDLT
HHHHHHHHHHCCCCC
34.0618525581
15PhosphorylationLKKMVSKYKYRDLTV
HHHHHHHHHCCCCCH
13.0220068231
16AcetylationKKMVSKYKYRDLTVR
HHHHHHHHCCCCCHH
37.2318525589
32PhosphorylationTVNVITLYKDLKPVL
HEEEEEEECCHHHHH
8.19-
48PhosphorylationSYVFNDGSSRELMNL
HEECCCCCCCCHHHC
29.1430108239
49UbiquitinationYVFNDGSSRELMNLT
EECCCCCCCCHHHCC
34.9927667366
49PhosphorylationYVFNDGSSRELMNLT
EECCCCCCCCHHHCC
34.9930108239
56PhosphorylationSRELMNLTGTIPVPY
CCCHHHCCCCCCCCC
27.5521214269
63PhosphorylationTGTIPVPYRGNTYNI
CCCCCCCCCCCCCCC
31.2421214269
90AcetylationNPPICFVKPTSSMTI
CCCEEEECCCCCCEE
23.4820167786
101UbiquitinationSMTIKTGKHVDANGK
CCEEECCCCCCCCCE
45.7627667366
110PhosphorylationVDANGKIYLPYLHEW
CCCCCEEECCCHHHC
12.7123898821
132 (in isoform 2)Ubiquitination-2.2221890473
152 (in isoform 2)Ubiquitination-26.1521890473
185UbiquitinationYPPNPSGYPGCPYPP
CCCCCCCCCCCCCCC
10.7821890473
191UbiquitinationGYPGCPYPPGGPYPA
CCCCCCCCCCCCCCC
13.2523000965
205UbiquitinationATTSSQYPSQPPVTT
CCCCCCCCCCCCEEE
20.8921890473
217UbiquitinationVTTVGPSRDGTISED
EEEECCCCCCCCCHH
49.8924816145
220PhosphorylationVGPSRDGTISEDTIR
ECCCCCCCCCHHHHH
26.1423401153
222PhosphorylationPSRDGTISEDTIRAS
CCCCCCCCHHHHHHH
29.2920873877
225PhosphorylationDGTISEDTIRASLIS
CCCCCHHHHHHHHHH
14.3326552605
229PhosphorylationSEDTIRASLISAVSD
CHHHHHHHHHHHHHH
19.1820873877
232PhosphorylationTIRASLISAVSDKLR
HHHHHHHHHHHHHHH
28.1029759185
235PhosphorylationASLISAVSDKLRWRM
HHHHHHHHHHHHHHH
28.8320873877
237 (in isoform 1)Ubiquitination-32.2321890473
237UbiquitinationLISAVSDKLRWRMKE
HHHHHHHHHHHHHHH
32.2323000965
237AcetylationLISAVSDKLRWRMKE
HHHHHHHHHHHHHHH
32.2323236377
243UbiquitinationDKLRWRMKEEMDRAQ
HHHHHHHHHHHHHHH
41.7823000965
256 (in isoform 2)Ubiquitination-3.6221890473
257UbiquitinationQAELNALKRTEEDLK
HHHHHHHHHCHHHHH
55.6622817900
257 (in isoform 1)Ubiquitination-55.6621890473
269UbiquitinationDLKKGHQKLEEMVTR
HHHHHHHHHHHHHHH
52.7924816145
286UbiquitinationQEVAEVDKNIELLKK
HHHHHHHHHHHHHHH
66.0729967540
292UbiquitinationDKNIELLKKKDEELS
HHHHHHHHHHHHHHH
71.1033845483
2922-HydroxyisobutyrylationDKNIELLKKKDEELS
HHHHHHHHHHHHHHH
71.10-
293UbiquitinationKNIELLKKKDEELSS
HHHHHHHHHHHHHHH
66.4829967540
294UbiquitinationNIELLKKKDEELSSA
HHHHHHHHHHHHHHH
69.6429967540
299PhosphorylationKKKDEELSSALEKME
HHHHHHHHHHHHHHH
19.4920068231
300PhosphorylationKKDEELSSALEKMEN
HHHHHHHHHHHHHHH
49.8820068231
304UbiquitinationELSSALEKMENQSEN
HHHHHHHHHHHCCCC
52.9829967540
309UbiquitinationLEKMENQSENNDIDE
HHHHHHCCCCCCCCC
54.6021890473
309PhosphorylationLEKMENQSENNDIDE
HHHHHHCCCCCCCCC
54.6029507054
330UbiquitinationPLYKQILNLYAEENA
HHHHHHHHHHHHHCC
32.4124816145
361UbiquitinationIDLDVFLKHVRLLSR
CCHHHHHHHHHHHCH
28.7022817900
361 (in isoform 1)Ubiquitination-28.7021890473
379UbiquitinationQLRALMQKARKTAGL
HHHHHHHHHHHHCCC
35.8729967540
379AcetylationQLRALMQKARKTAGL
HHHHHHHHHHHHCCC
35.8725953088
382UbiquitinationALMQKARKTAGLSDL
HHHHHHHHHCCCCCC
47.8124816145
387PhosphorylationARKTAGLSDLY----
HHHHCCCCCCC----
25.3424719451
390PhosphorylationTAGLSDLY-------
HCCCCCCC-------
22.8419605366

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
-KUbiquitinationE3 ubiquitin ligaseMGRN1O60291
PMID:17229889
-KUbiquitinationE3 ubiquitin ligaseLRSAM1Q6UWE0
PMID:15256501
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:15126635
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:18321968

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TS101_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 TS101_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDN1A_HUMANCDKN1Aphysical
11943869
LIPB2_HUMANPPFIBP2physical
16189514
LRSM1_HUMANLRSAM1physical
16189514
CEP55_HUMANCEP55physical
16189514
VPS28_HUMANVPS28physical
16189514
HGS_HUMANHGSphysical
16189514
VP37C_HUMANVPS37Cphysical
15509564
KIF5A_HUMANKIF5Aphysical
15256501
ITSN1_HUMANITSN1physical
15256501
LRSM1_HUMANLRSAM1physical
15256501
VP37A_HUMANVPS37Aphysical
15218037
VP37B_HUMANVPS37Bphysical
15218037
VPS28_HUMANVPS28physical
15218037
HGS_HUMANHGSphysical
12802020
EP300_HUMANEP300physical
10440698
VPS28_HUMANVPS28physical
11134028
P53_HUMANTP53physical
11172000
MDM2_HUMANMDM2physical
11172000
BCR_HUMANBCRphysical
16778200
RN126_HUMANRNF126physical
19549727
TRAIP_HUMANTRAIPphysical
19549727
RNF41_HUMANRNF41physical
19549727
LRSM1_HUMANLRSAM1physical
19549727
DZIP3_HUMANDZIP3physical
19549727
MGRN1_HUMANMGRN1physical
19549727
MKRN3_HUMANMKRN3physical
19549727
TRI23_HUMANTRIM23physical
19549727
TRI74_HUMANTRIM74physical
19549727
TRI35_HUMANTRIM35physical
19549727
VPS11_HUMANVPS11physical
19549727
RAD18_HUMANRAD18physical
19549727
RN111_HUMANRNF111physical
19549727
TRI46_HUMANTRIM46physical
19549727
GAG_HV1H2gagphysical
16434471
LRSM1_HUMANLRSAM1physical
18077552
MGRN1_HUMANMGRN1physical
17229889
TNNT3_HUMANTNNT3physical
15604093
MGRN1_HUMANMGRN1physical
19703557
GAG_HV2BEgag-polphysical
12388682
SNF8_HUMANSNF8physical
16973552
VPS36_HUMANVPS36physical
16973552
TS101_HUMANTSG101physical
16973552
GAG_HV1H2gagphysical
21070952
HGS_HUMANHGSphysical
21070952
TS101_HUMANTSG101physical
19542561
VP37B_HUMANVPS37Bphysical
19542561
HGS_HUMANHGSphysical
19542561
PDC6I_HUMANPDCD6IPphysical
19542561
ATX2_HUMANATXN2physical
19542561
BAG6_HUMANBAG6physical
19542561
CAPR1_HUMANCAPRIN1physical
19542561
CPSF7_HUMANCPSF7physical
19542561
DDX6_HUMANDDX6physical
19542561
EWS_HUMANEWSR1physical
19542561
FAS_HUMANFASNphysical
19542561
HNRL1_HUMANHNRNPUL1physical
19542561
IF4B_HUMANEIF4Bphysical
19542561
LARP1_HUMANLARP1physical
19542561
LRSM1_HUMANLRSAM1physical
19542561
NFKB2_HUMANNFKB2physical
19542561
NONO_HUMANNONOphysical
19542561
NUFP2_HUMANNUFIP2physical
19542561
ODP2_HUMANDLATphysical
19542561
PABP1_HUMANPABPC1physical
19542561
PABP4_HUMANPABPC4physical
19542561
RENT1_HUMANUPF1physical
19542561
S23IP_HUMANSEC23IPphysical
19542561
SC16A_HUMANSEC16Aphysical
19542561
SC24B_HUMANSEC24Bphysical
19542561
SFPQ_HUMANSFPQphysical
19542561
TB182_HUMANTNKS1BP1physical
19542561
TFG_HUMANTFGphysical
19542561
TRI47_HUMANTRIM47physical
19542561
UBC_HUMANUBCphysical
19542561
VASP_HUMANVASPphysical
19542561
WDR26_HUMANWDR26physical
19542561
UBC_HUMANUBCphysical
15053872
GAG_HV1H2gagphysical
14581525
GAG_HV1H2gagphysical
12900394
TS101_HUMANTSG101physical
12900394
HGS_HUMANHGSphysical
12900394
GAG_HV1H2gagphysical
12379843
GAG_HV1H2gagphysical
11595185
ASZ1_HUMANASZ1physical
21880841
AKAP9_HUMANAKAP9physical
18643869
CEP55_HUMANCEP55physical
17853893
IQGA1_HUMANIQGAP1physical
17853893
ROCK1_HUMANROCK1physical
17853893
CD2AP_HUMANCD2APphysical
17853893
MDM2_HUMANMDM2physical
17060450
NEDD4_HUMANNEDD4physical
16138902
GAG_HV1H2gagphysical
16138902
GCR_HUMANNR3C1physical
15657031
TM1L1_HUMANTOM1L1physical
15611048
DAXX_HUMANDAXXphysical
15033475
HGS_HUMANHGSphysical
12900395
VPS28_HUMANVPS28physical
12663786
TS101_HUMANTSG101physical
12663786
GAG_HV1H2gagphysical
11427703
GAG_HV1H2gagphysical
21159863
PDC6I_HUMANPDCD6IPphysical
20929444
HGS_HUMANHGSphysical
17182674
UBAP1_HUMANUBAP1physical
21757351
VP37A_HUMANVPS37Aphysical
21757351
VP37C_HUMANVPS37Cphysical
21757351
RFIP4_HUMANRAB11FIP4physical
22348143
RFIP3_HUMANRAB11FIP3physical
22348143
GAG_SIVG1gag-polphysical
15163754
ARRD1_HUMANARRDC1physical
22315426
UBAP1_HUMANUBAP1physical
22405001
VP37A_HUMANVPS37Aphysical
22405001
VP37B_HUMANVPS37Bphysical
22405001
VP37B_HUMANVPS37Bphysical
22939629
XPO1_HUMANXPO1physical
22939629
WDR12_HUMANWDR12physical
22939629
UBAP1_HUMANUBAP1physical
24284069
VPS28_HUMANVPS28physical
24284069
VP37A_HUMANVPS37Aphysical
24284069
VP37C_HUMANVPS37Cphysical
24284069
MB12A_HUMANMVB12Aphysical
24284069
ANDR_HUMANARphysical
23146908
DAPK3_HUMANDAPK3physical
23146908
AATF_HUMANAATFphysical
23146908
TAXB1_HUMANTAX1BP1physical
25416956
PDLI7_HUMANPDLIM7physical
25416956
MGRN1_HUMANMGRN1physical
25416956
VPS28_HUMANVPS28physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
CEP55_HUMANCEP55physical
25416956
USBP1_HUMANUSHBP1physical
25416956
LRSM1_HUMANLRSAM1physical
25416956
SYCE1_HUMANSYCE1physical
25416956
HAUS1_HUMANHAUS1physical
25416956
VP37A_HUMANVPS37Aphysical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
ZFYV9_HUMANZFYVE9physical
23222715
GAG_HV1H2gagphysical
12006492
UBC_HUMANUBCphysical
12006492
AACS_HUMANAACSphysical
26344197
ACTN4_HUMANACTN4physical
26344197
ARFG2_HUMANARFGAP2physical
26344197
DNJB1_HUMANDNAJB1physical
26344197
DPH2_HUMANDPH2physical
26344197
DPYL2_HUMANDPYSL2physical
26344197
HIP1R_HUMANHIP1Rphysical
26344197
NDRG1_HUMANNDRG1physical
26344197
NIF3L_HUMANNIF3L1physical
26344197
PALLD_HUMANPALLDphysical
26344197
SYSC_HUMANSARSphysical
26344197
SH3K1_HUMANSH3KBP1physical
26344197
SMHD1_HUMANSMCHD1physical
26344197
TATD1_HUMANTATDN1physical
26344197
TRI25_HUMANTRIM25physical
26344197
UBAP1_HUMANUBAP1physical
26344197
UBC9_HUMANUBE2Iphysical
26344197
VPS28_HUMANVPS28physical
26344197
VP37B_HUMANVPS37Bphysical
26344197
VP37C_HUMANVPS37Cphysical
26344197
SYWC_HUMANWARSphysical
26344197
VP37A_HUMANVPS37Aphysical
15604093
BCAS3_HUMANBCAS3physical
25640309
KLK5_HUMANKLK5physical
25640309
KLK6_HUMANKLK6physical
25640309
MTA3_HUMANMTA3physical
25640309
RSLAB_HUMANRASL10Bphysical
25640309
SG3A1_HUMANSCGB3A1physical
25640309
TFF1_HUMANTFF1physical
25640309
THRSP_HUMANTHRSPphysical
25640309
TSP50_HUMANPRSS50physical
25640309
TS101_HUMANTSG101physical
25330247
LRSM1_HUMANLRSAM1physical
26811492
YBOX1_HUMANYBX1physical
26343856
GB_HHV8PORF8physical
27764233
CBL_HUMANCBLphysical
27764233
BCAR1_HUMANBCAR1physical
27764233
CRK_HUMANCRKphysical
27764233
EPHA2_HUMANEPHA2physical
27764233
RAB5A_HUMANRAB5Aphysical
27764233
RAB7A_HUMANRAB7Aphysical
27764233
HGS_HUMANHGSphysical
27764233
VPS36_HUMANVPS36physical
27764233
CHMP6_HUMANCHMP6physical
27764233
CHMP5_HUMANCHMP5physical
27764233
URFB1_HUMANUHRF1BP1physical
27173435
GAG_HV1H2gagphysical
27648839

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 TS101_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-390, AND MASSSPECTROMETRY.

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