TTC5_HUMAN - dbPTM
TTC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC5_HUMAN
UniProt AC Q8N0Z6
Protein Name Tetratricopeptide repeat protein 5
Gene Name TTC5
Organism Homo sapiens (Human).
Sequence Length 440
Subcellular Localization Nucleus. Cytoplasm. Phosphorylation at Ser-203 results in nuclear localization, while unphosphorylated protein localizes to the cytoplasm..
Protein Description Adapter protein involved in p53/TP53 response that acts by regulating and mediating the assembly of multi-protein complexes. Required to facilitate the interaction between JMY and p300/EP300 and increase p53/TP53-dependent transcription and apoptosis. Prevents p53/TP53 degradation by MDM2 (By similarity)..
Protein Sequence MMADEEEEVKPILQKLQELVDQLYSFRDCYFETHSVEDAGRKQQDVQKEMEKTLQQMEEVVGSVQGKAQVLMLTGKALNVTPDYSPKAEELLSKAVKLEPELVEAWNQLGEVYWKKGDVAAAHTCFSGALTHCRNKVSLQNLSMVLRQLRTDTEDEHSHHVMDSVRQAKLAVQMDVHDGRSWYILGNSYLSLYFSTGQNPKISQQALSAYAQAEKVDRKASSNPDLHLNRATLHKYEESYGEALEGFSRAAALDPAWPEPRQREQQLLEFLDRLTSLLESKGKVKTKKLQSMLGSLRPAHLGPCSDGHYQSASGQKVTLELKPLSTLQPGVNSGAVILGKVVFSLTTEEKVPFTFGLVDSDGPCYAVMVYNIVQSWGVLIGDSVAIPEPNLRLHRIQHKGKDYSFSSVRVETPLLLVVNGKPQGSSSQAVATVASRPQCE
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
52UbiquitinationDVQKEMEKTLQQMEE
HHHHHHHHHHHHHHH
53.90-
74O-linked_GlycosylationKAQVLMLTGKALNVT
CEEEEEEECCCCCCC
23.7530379171
76UbiquitinationQVLMLTGKALNVTPD
EEEEEECCCCCCCCC
44.45-
81PhosphorylationTGKALNVTPDYSPKA
ECCCCCCCCCCCHHH
14.9030301811
84PhosphorylationALNVTPDYSPKAEEL
CCCCCCCCCHHHHHH
28.2430301811
85PhosphorylationLNVTPDYSPKAEELL
CCCCCCCCHHHHHHH
27.5721815630
87UbiquitinationVTPDYSPKAEELLSK
CCCCCCHHHHHHHHH
63.59-
94UbiquitinationKAEELLSKAVKLEPE
HHHHHHHHHCCCCHH
58.11-
94AcetylationKAEELLSKAVKLEPE
HHHHHHHHHCCCCHH
58.1121466224
97UbiquitinationELLSKAVKLEPELVE
HHHHHHCCCCHHHHH
52.58-
97SumoylationELLSKAVKLEPELVE
HHHHHHCCCCHHHHH
52.58-
115UbiquitinationQLGEVYWKKGDVAAA
HHCCEEECCCCHHHH
29.23-
136UbiquitinationALTHCRNKVSLQNLS
HHHHHCCCHHHHHHH
17.53-
138PhosphorylationTHCRNKVSLQNLSMV
HHHCCCHHHHHHHHH
26.33-
151PhosphorylationMVLRQLRTDTEDEHS
HHHHHHCCCCCCCHH
56.7325944883
153PhosphorylationLRQLRTDTEDEHSHH
HHHHCCCCCCCHHHH
44.7325944883
158PhosphorylationTDTEDEHSHHVMDSV
CCCCCCHHHHHHHHH
17.1522985185
164PhosphorylationHSHHVMDSVRQAKLA
HHHHHHHHHHHHEEE
10.9125944883
193PhosphorylationGNSYLSLYFSTGQNP
CCEEEEEEEECCCCC
7.66-
203PhosphorylationTGQNPKISQQALSAY
CCCCCCCCHHHHHHH
23.5121082442
210PhosphorylationSQQALSAYAQAEKVD
CHHHHHHHHHHHHHH
8.8927642862
215UbiquitinationSAYAQAEKVDRKASS
HHHHHHHHHHHHHHC
53.07-
219UbiquitinationQAEKVDRKASSNPDL
HHHHHHHHHHCCCCC
48.43-
221PhosphorylationEKVDRKASSNPDLHL
HHHHHHHHCCCCCCC
33.41-
235UbiquitinationLNRATLHKYEESYGE
CCHHHHHHHHHHHHH
58.43-
236PhosphorylationNRATLHKYEESYGEA
CHHHHHHHHHHHHHH
17.7422817900
283UbiquitinationSLLESKGKVKTKKLQ
HHHHHCCCCCHHHHH
44.27-
288UbiquitinationKGKVKTKKLQSMLGS
CCCCCHHHHHHHHHC
57.92-
295PhosphorylationKLQSMLGSLRPAHLG
HHHHHHHCCCCHHCC
19.7624719451
322SumoylationQKVTLELKPLSTLQP
CEEEEEEEECCCCCC
34.24-
401UbiquitinationHRIQHKGKDYSFSSV
EEEEECCCCCCCCCE
59.29-

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 TTC5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
203SPhosphorylation

-

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 TTC5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCR_HUMANNR3C1physical
21147850
ANDR_HUMANARphysical
21147850
ESR1_HUMANESR1physical
21147850
MYC_HUMANMYCphysical
23559008
GMDS_HUMANGMDSphysical
26344197
HYI_HUMANHYIphysical
26344197
SPB8_HUMANSERPINB8physical
26344197
ZBTB9_HUMANZBTB9physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
T11L2_HUMANTCP11L2physical
28514442
NLGN2_HUMANNLGN2physical
28514442
TBB8_HUMANTUBB8physical
28514442
T11L1_HUMANTCP11L1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTC5_HUMAN

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Related Literatures of Post-Translational Modification

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