TRIM4_HUMAN - dbPTM
TRIM4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM4_HUMAN
UniProt AC Q9C037
Protein Name E3 ubiquitin-protein ligase TRIM4
Gene Name TRIM4
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn't lead to proteasomal degradation but seems to enhance IFN induction..
Protein Sequence MEAEDIQEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGGGPFPCPECRHPSAPAALRPNWALARLTEKTQRRRLGPVPPGLCGRHWEPLRLFCEDDQRPVCLVCRESQEHQTHAMAPIDEAFESYRTGNFDIHVDEWKRRLIRLLLYHFKQEEKLLKSQRNLVAKMKKVMHLQDVEVKNATQWKDKIKSQRMRISTEFSKLHNFLVEEEDLFLQRLNKEEEETKKKLNENTLKLNQTIASLKKLILEVGEKSQAPTLELLQNPKEVLTRSEIQDVNYSLEAVKVKTVCQIPLMKEMLKRFQVAVNLAEDTAHPKLVFSQEGRYVKNTASASSWPVFSSAWNYFAGWRNPQKTAFVERFQHLPCVLGKNVFTSGKHYWEVESRDSLEVAVGVCREDVMGITDRSKMSPDVGIWAIYWSAAGYWPLIGFPGTPTQQEPALHRVGVYLDRGTGNVSFYSAVDGVHLHTFSCSSVSRLRPFFWLSPLASLVIPPVTDRK
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
56PhosphorylationCPECRHPSAPAALRP
CCCCCCCCCCCHHCC
40.5327251275
73 (in isoform 2)Ubiquitination-44.7322053931
73UbiquitinationALARLTEKTQRRRLG
HHHHHHHHHHHHCCC
44.7322053931
129 (in isoform 3)Phosphorylation-17.29-
129 (in isoform 2)Phosphorylation-17.29-
130 (in isoform 3)Phosphorylation-12.66-
130 (in isoform 2)Phosphorylation-12.66-
147UbiquitinationDEWKRRLIRLLLYHF
HHHHHHHHHHHHHHH
2.5029967540
152PhosphorylationRLIRLLLYHFKQEEK
HHHHHHHHHHHHHHH
12.7419658100
157 (in isoform 3)Ubiquitination-58.6621906983
157 (in isoform 2)Ubiquitination-58.6622053931
157UbiquitinationLLYHFKQEEKLLKSQ
HHHHHHHHHHHHHHH
58.6632015554
163UbiquitinationQEEKLLKSQRNLVAK
HHHHHHHHHHHHHHH
34.0527667366
173AcetylationNLVAKMKKVMHLQDV
HHHHHHHHHHHHHCC
41.0922424773
173UbiquitinationNLVAKMKKVMHLQDV
HHHHHHHHHHHHHCC
41.0929967540
183 (in isoform 1)Ubiquitination-27.6221906983
183UbiquitinationHLQDVEVKNATQWKD
HHHCCCCCCCHHHHH
27.6221906983
189UbiquitinationVKNATQWKDKIKSQR
CCCCHHHHHHHHHHH
39.0527667366
197UbiquitinationDKIKSQRMRISTEFS
HHHHHHHHHHHHHHH
3.2833845483
200PhosphorylationKSQRMRISTEFSKLH
HHHHHHHHHHHHHHH
16.1224719451
205UbiquitinationRISTEFSKLHNFLVE
HHHHHHHHHHHHHHC
60.1229967540
212UbiquitinationKLHNFLVEEEDLFLQ
HHHHHHHCHHHHHHH
58.7929967540
221UbiquitinationEDLFLQRLNKEEEET
HHHHHHHHCHHHHHH
7.4733845483
221 (in isoform 3)Ubiquitination-7.4721906983
221 (in isoform 2)Ubiquitination-7.4722053931
222UbiquitinationDLFLQRLNKEEEETK
HHHHHHHCHHHHHHH
52.4633845483
223UbiquitinationLFLQRLNKEEEETKK
HHHHHHCHHHHHHHH
71.7133845483
230UbiquitinationKEEEETKKKLNENTL
HHHHHHHHHHCHHHH
70.6629967540
231UbiquitinationEEEETKKKLNENTLK
HHHHHHHHHCHHHHH
59.0929967540
236PhosphorylationKKKLNENTLKLNQTI
HHHHCHHHHHHHHHH
21.0629978859
238UbiquitinationKLNENTLKLNQTIAS
HHCHHHHHHHHHHHH
43.2729967540
243 (in isoform 2)Ubiquitination-1.4422053931
243UbiquitinationTLKLNQTIASLKKLI
HHHHHHHHHHHHHHH
1.4423503661
243 (in isoform 3)Ubiquitination-1.4421906983
245PhosphorylationKLNQTIASLKKLILE
HHHHHHHHHHHHHHH
36.5524719451
247AcetylationNQTIASLKKLILEVG
HHHHHHHHHHHHHHH
42.9325953088
2472-HydroxyisobutyrylationNQTIASLKKLILEVG
HHHHHHHHHHHHHHH
42.93-
247 (in isoform 1)Ubiquitination-42.9321906983
247UbiquitinationNQTIASLKKLILEVG
HHHHHHHHHHHHHHH
42.9321906983
248UbiquitinationQTIASLKKLILEVGE
HHHHHHHHHHHHHHH
46.1633845483
256UbiquitinationLILEVGEKSQAPTLE
HHHHHHHHCCCCHHH
41.7729967540
262 (in isoform 3)Ubiquitination-4.2021906983
262UbiquitinationEKSQAPTLELLQNPK
HHCCCCHHHHHCCHH
4.2033845483
262 (in isoform 2)Ubiquitination-4.2022053931
264UbiquitinationSQAPTLELLQNPKEV
CCCCHHHHHCCHHHH
7.2023503661
269 (in isoform 1)Ubiquitination-68.9221906983
269UbiquitinationLELLQNPKEVLTRSE
HHHHCCHHHHHCHHH
68.9221906983
273PhosphorylationQNPKEVLTRSEIQDV
CCHHHHHCHHHHCCC
37.0129759185
275PhosphorylationPKEVLTRSEIQDVNY
HHHHHCHHHHCCCCC
33.5429759185
282PhosphorylationSEIQDVNYSLEAVKV
HHHCCCCCCCEECEE
17.9329759185
288 (in isoform 1)Ubiquitination-45.0921906983
288UbiquitinationNYSLEAVKVKTVCQI
CCCCEECEEEEEHHC
45.0921906983
290UbiquitinationSLEAVKVKTVCQIPL
CCEECEEEEEHHCHH
29.5323503661
304UbiquitinationLMKEMLKRFQVAVNL
HHHHHHHHHHHHHHH
24.2222817900
319UbiquitinationAEDTAHPKLVFSQEG
CCCCCCCEEEECCCC
47.63-
330 (in isoform 2)Ubiquitination-39.3822053931
330UbiquitinationSQEGRYVKNTASASS
CCCCCEEECCCCHHC
39.3833845483
334PhosphorylationRYVKNTASASSWPVF
CEEECCCCHHCCCCC
27.0124275569
337PhosphorylationKNTASASSWPVFSSA
ECCCCHHCCCCCHHH
34.8124275569
342PhosphorylationASSWPVFSSAWNYFA
HHCCCCCHHHHHHHC
21.2724275569
343PhosphorylationSSWPVFSSAWNYFAG
HCCCCCHHHHHHHCC
26.3224275569
346UbiquitinationPVFSSAWNYFAGWRN
CCCHHHHHHHCCCCC
23.0429967540
353UbiquitinationNYFAGWRNPQKTAFV
HHHCCCCCHHCCHHH
36.5223503661
353 (in isoform 2)Ubiquitination-36.52-
356 (in isoform 1)Ubiquitination-42.9821906983
356UbiquitinationAGWRNPQKTAFVERF
CCCCCHHCCHHHHHH
42.9827667366
372UbiquitinationHLPCVLGKNVFTSGK
CCCEEEECCCCCCCC
45.8629967540
376PhosphorylationVLGKNVFTSGKHYWE
EEECCCCCCCCCEEE
32.0824905233
377PhosphorylationLGKNVFTSGKHYWEV
EECCCCCCCCCEEEE
34.0924905233
379UbiquitinationKNVFTSGKHYWEVES
CCCCCCCCCEEEEEC
33.0323503661
381PhosphorylationVFTSGKHYWEVESRD
CCCCCCCEEEEECCC
13.5229496907
386PhosphorylationKHYWEVESRDSLEVA
CCEEEEECCCHHEEE
46.7124905233
405PhosphorylationREDVMGITDRSKMSP
HHHHCCCCCHHHCCC
21.4520071362

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 TRIM4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM4_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 TRIM4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM4_HUMANTRIM4physical
17156811
TRIM4_HUMANTRIM4physical
21680743
PDIA1_HUMANP4HBphysical
26186194
PRDX1_HUMANPRDX1physical
26524401
PDIA1_HUMANP4HBphysical
28514442

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 TRIM4_HUMAN

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Related Literatures of Post-Translational Modification

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