TLS1_HUMAN - dbPTM
TLS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLS1_HUMAN
UniProt AC Q9NZ63
Protein Name Telomere length and silencing protein 1 homolog {ECO:0000250|UniProtKB:Q10148}
Gene Name C9orf78
Organism Homo sapiens (Human).
Sequence Length 289
Subcellular Localization
Protein Description Involved in the regulation of telomeric heterochromatin assembly and control of telomere length..
Protein Sequence MPVVRKIFRRRRGDSESEEDEQDSEEVRLKLEETREVQNLRKRPNGVSAVALLVGEKVQEETTLVDDPFQMKTGGMVDMKKLKERGKDKISEEEDLHLGTSFSAETNRRDEDADMMKYIETELKKRKGIVEHEEQKVKPKNAEDCLYELPENIRVSSAKKTEEMLSNQMLSGIPEVDLGIDAKIKNIISTEDAKARLLAEQQNKKKDSETSFVPTNMAVNYVQHNRFYHEELNAPIRRNKEEPKARPLRVGDTEKPEPERSPPNRKRPANEKATDDYHYEKFKKMNRRY
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
15PhosphorylationFRRRRGDSESEEDEQ
HHHHCCCCCCCCCCC
29255136
17PhosphorylationRRRGDSESEEDEQDS
HHCCCCCCCCCCCCC
29255136
24PhosphorylationSEEDEQDSEEVRLKL
CCCCCCCCHHHHHHH
20164059
30UbiquitinationDSEEVRLKLEETREV
CCHHHHHHHHHHHHH
29967540
48PhosphorylationRKRPNGVSAVALLVG
HHCCCCCHHHHHHHC
28555341
62PhosphorylationGEKVQEETTLVDDPF
CCCCCCCCEECCCCC
25463755
63PhosphorylationEKVQEETTLVDDPFQ
CCCCCCCEECCCCCC
25463755
71SulfoxidationLVDDPFQMKTGGMVD
ECCCCCCCCCCCCCC
21406390
72UbiquitinationVDDPFQMKTGGMVDM
CCCCCCCCCCCCCCH
32015554
73PhosphorylationDDPFQMKTGGMVDMK
CCCCCCCCCCCCCHH
25463755
80AcetylationTGGMVDMKKLKERGK
CCCCCCHHHHHHHCC
25953088
91PhosphorylationERGKDKISEEEDLHL
HHCCCCCCHHHHCCC
28985074
97UbiquitinationISEEEDLHLGTSFSA
CCHHHHCCCCCCCCC
24816145
100PhosphorylationEEDLHLGTSFSAETN
HHHCCCCCCCCCCCC
25159151
101PhosphorylationEDLHLGTSFSAETNR
HHCCCCCCCCCCCCC
25159151
103PhosphorylationLHLGTSFSAETNRRD
CCCCCCCCCCCCCCC
26074081
106PhosphorylationGTSFSAETNRRDEDA
CCCCCCCCCCCCCCH
26074081
117UbiquitinationDEDADMMKYIETELK
CCCHHHHHHHHHHHH
24816145
118PhosphorylationEDADMMKYIETELKK
CCHHHHHHHHHHHHH
28796482
118UbiquitinationEDADMMKYIETELKK
CCHHHHHHHHHHHHH
24816145
121PhosphorylationDMMKYIETELKKRKG
HHHHHHHHHHHHCCC
20068231
124UbiquitinationKYIETELKKRKGIVE
HHHHHHHHHCCCCCC
29967540
125UbiquitinationYIETELKKRKGIVEH
HHHHHHHHCCCCCCC
-
127AcetylationETELKKRKGIVEHEE
HHHHHHCCCCCCCCH
7681437
136UbiquitinationIVEHEEQKVKPKNAE
CCCCCHHCCCCCCHH
33845483
136AcetylationIVEHEEQKVKPKNAE
CCCCCHHCCCCCCHH
7681447
138UbiquitinationEHEEQKVKPKNAEDC
CCCHHCCCCCCHHHH
24816145
140UbiquitinationEEQKVKPKNAEDCLY
CHHCCCCCCHHHHHH
33845483
147PhosphorylationKNAEDCLYELPENIR
CCHHHHHHHCCCCCC
21945579
156PhosphorylationLPENIRVSSAKKTEE
CCCCCCCCCCHHHHH
30576142
157PhosphorylationPENIRVSSAKKTEEM
CCCCCCCCCHHHHHH
30576142
160UbiquitinationIRVSSAKKTEEMLSN
CCCCCCHHHHHHHHH
29967540
161PhosphorylationRVSSAKKTEEMLSNQ
CCCCCHHHHHHHHHH
21712546
164SulfoxidationSAKKTEEMLSNQMLS
CCHHHHHHHHHHHHC
21406390
185UbiquitinationLGIDAKIKNIISTED
CCCCHHHHCCCCCHH
24816145
1852-HydroxyisobutyrylationLGIDAKIKNIISTED
CCCCHHHHCCCCCHH
-
194UbiquitinationIISTEDAKARLLAEQ
CCCCHHHHHHHHHHH
33845483
1942-HydroxyisobutyrylationIISTEDAKARLLAEQ
CCCCHHHHHHHHHHH
-
204UbiquitinationLLAEQQNKKKDSETS
HHHHHHHCCCCCCCC
29967540
2042-HydroxyisobutyrylationLLAEQQNKKKDSETS
HHHHHHHCCCCCCCC
-
205UbiquitinationLAEQQNKKKDSETSF
HHHHHHCCCCCCCCC
24816145
208PhosphorylationQQNKKKDSETSFVPT
HHHCCCCCCCCCCCH
28555341
210PhosphorylationNKKKDSETSFVPTNM
HCCCCCCCCCCCHHH
28555341
211PhosphorylationKKKDSETSFVPTNMA
CCCCCCCCCCCHHHH
28555341
215PhosphorylationSETSFVPTNMAVNYV
CCCCCCCHHHHHHHH
26552605
221PhosphorylationPTNMAVNYVQHNRFY
CHHHHHHHHHCCCHH
28796482
224UbiquitinationMAVNYVQHNRFYHEE
HHHHHHHCCCHHHHH
24816145
226MethylationVNYVQHNRFYHEELN
HHHHHCCCHHHHHHC
-
228PhosphorylationYVQHNRFYHEELNAP
HHHCCCHHHHHHCCC
28796482
235UbiquitinationYHEELNAPIRRNKEE
HHHHHCCCCCCCCCC
24816145
244UbiquitinationRRNKEEPKARPLRVG
CCCCCCCCCCCCCCC
24816145
252UbiquitinationARPLRVGDTEKPEPE
CCCCCCCCCCCCCCC
24816145
253PhosphorylationRPLRVGDTEKPEPER
CCCCCCCCCCCCCCC
29255136
255UbiquitinationLRVGDTEKPEPERSP
CCCCCCCCCCCCCCC
24816145
261PhosphorylationEKPEPERSPPNRKRP
CCCCCCCCCCCCCCC
29255136
272UbiquitinationRKRPANEKATDDYHY
CCCCCCCCCCCHHHH
24816145
274PhosphorylationRPANEKATDDYHYEK
CCCCCCCCCHHHHHH
26074081
277PhosphorylationNEKATDDYHYEKFKK
CCCCCCHHHHHHHHH
28796482
279PhosphorylationKATDDYHYEKFKKMN
CCCCHHHHHHHHHHH
28796482
281UbiquitinationTDDYHYEKFKKMNRR
CCHHHHHHHHHHHHC
29967540
281AcetylationTDDYHYEKFKKMNRR
CCHHHHHHHHHHHHC
27452117

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 ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLS1_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 TLS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
FKBP9_HUMANFKBP9physical
22863883
HERC4_HUMANHERC4physical
22863883
LIMD1_HUMANLIMD1physical
22863883
NUBP2_HUMANNUBP2physical
22863883
UBR7_HUMANUBR7physical
22863883
OCRL_HUMANOCRLphysical
26186194
CE120_HUMANCEP120physical
26186194
BTBD1_HUMANBTBD1physical
26186194
BTBD2_HUMANBTBD2physical
26186194
SYHC_HUMANHARSphysical
26344197
HNRH1_HUMANHNRNPH1physical
26344197
TLS1_HUMANC9orf78physical
26472760
U5S1_HUMANEFTUD2physical
26472760
U520_HUMANSNRNP200physical
26472760
PRP8_HUMANPRPF8physical
26472760
CE120_HUMANCEP120physical
28514442
BTBD1_HUMANBTBD1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLS1_HUMAN

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Related Literatures of Post-Translational Modification

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