TRI69_HUMAN - dbPTM
TRI69_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI69_HUMAN
UniProt AC Q86WT6
Protein Name E3 ubiquitin-protein ligase TRIM69
Gene Name TRIM69
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Cytoplasm . Nucleus . Nucleus speckle .
Protein Description May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis..
Protein Sequence MEVSTNPSSNIDPGDYVEMNDSITHLPSKVVIQDITMELHCPLCNDWFRDPLMLSCGHNFCEACIQDFWRLQAKETFCPECKMLCQYNNCTFNPVLDKLVEKIKKLPLLKGHPQCPEHGENLKLFSKPDGKLICFQCKDARLSVGQSKEFLQISDAVHFFTEELAIQQGQLETTLKELQTLRNMQKEAIAAHKENKLHLQQHVSMEFLKLHQFLHSKEKDILTELREEGKALNEEMELNLSQLQEQCLLAKDMLVSIQAKTEQQNSFDFLKDITTLLHSLEQGMKVLATRELISRKLNLGQYKGPIQYMVWREMQDTLCPGLSPLTLDPKTAHPNLVLSKSQTSVWHGDIKKIMPDDPERFDSSVAVLGSRGFTSGKWYWEVEVAKKTKWTVGVVRESIIRKGSCPLTPEQGFWLLRLRNQTDLKALDLPSFSLTLTNNLDKVGIYLDYEGGQLSFYNAKTMTHIYTFSNTFMEKLYPYFCPCLNDGGENKEPLHILHPQ
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
14 (in isoform 2)Phosphorylation-34.8224043423
15 (in isoform 2)Phosphorylation-50.0924043423
21 (in isoform 2)Phosphorylation-39.8624043423
28PhosphorylationDSITHLPSKVVIQDI
CCCCCCCCCEEEEEE
44.4324719451
126PhosphorylationGENLKLFSKPDGKLI
CCCCEEEECCCCCEE
54.4324719451
204PhosphorylationLHLQQHVSMEFLKLH
HHHHHHHHHHHHHHH
15.52-
289PhosphorylationQGMKVLATRELISRK
HHHHHHHHHHHHHHC
22.10-
294PhosphorylationLATRELISRKLNLGQ
HHHHHHHHHCCCCCC
35.6724719451
317PhosphorylationVWREMQDTLCPGLSP
HHHHHHHCCCCCCCC
17.23-
323PhosphorylationDTLCPGLSPLTLDPK
HCCCCCCCCCCCCCC
24.63-
341PhosphorylationPNLVLSKSQTSVWHG
CCEEECCCCCEEECC
35.00-
404PhosphorylationESIIRKGSCPLTPEQ
HHHHHCCCCCCCHHH
18.6525693802
408PhosphorylationRKGSCPLTPEQGFWL
HCCCCCCCHHHCEEE
15.2125693802

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 TRI69_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI69_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 TRI69_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PML_HUMANPMLphysical
12837286
A4_HUMANAPPphysical
21832049
TRI69_HUMANTRIM69physical
25416956
ZN483_HUMANZNF483physical
25416956
SYNE4_HUMANSYNE4physical
25416956
PPR18_HUMANPPP1R18physical
25416956
NEK8_HUMANNEK8physical
25416956
IYD1_HUMANIYDphysical
25416956
MAGA4_HUMANMAGEA4physical
21516116
AT5G1_HUMANATP5G1physical
21516116
RECK_HUMANRECKphysical
21516116
UB2E1_HUMANUBE2E1physical
23131556
UBE2H_HUMANUBE2Hphysical
23131556
UB2D1_HUMANUBE2D1physical
23131556
UB2D3_HUMANUBE2D3physical
23131556
UBE2N_HUMANUBE2Nphysical
23131556
DTBP1_HUMANDTNBP1physical
28514442
BL1S2_HUMANBLOC1S2physical
28514442
SNAPN_HUMANSNAPINphysical
28514442
BL1S5_HUMANBLOC1S5physical
28514442
TRIM4_HUMANTRIM4physical
28514442
RIR1_HUMANRRM1physical
28514442
POTEF_HUMANPOTEFphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI69_HUMAN

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Related Literatures of Post-Translational Modification

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