TRI14_HUMAN - dbPTM
TRI14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI14_HUMAN
UniProt AC Q14142
Protein Name Tripartite motif-containing protein 14
Gene Name TRIM14
Organism Homo sapiens (Human).
Sequence Length 442
Subcellular Localization Mitochondrion outer membrane .
Protein Description Plays a role in the innate immune defense against viruses. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways. [PubMed: 24379373 Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation]
Protein Sequence MAGAATGSRTPGRSELVEGCGWRCPEHGDRVAELFCRRCRRCVCALCPVLGAHRGHPVGLALEAAVHVQKLSQECLKQLAIKKQQHIDNITQIEDATEKLKANAESSKTWLKGKFTELRLLLDEEEALAKKFIDKNTQLTLQVYREQADSCREQLDIMNDLSNRVWSISQEPDPVQRLQAYTATEQEMQQQMSLGELCHPVPLSFEPVKSFFKGLVEAVESTLQTPLDIRLKESINCQLSDPSSTKPGTLLKTSPSPERSLLLKYARTPTLDPDTMHARLRLSADRLTVRCGLLGSLGPVPVLRFDALWQVLARDCFATGRHYWEVDVQEAGAGWWVGAAYASLRRRGASAAARLGCNRQSWCLKRYDLEYWAFHDGQRSRLRPRDDLDRLGVFLDYEAGVLAFYDVTGGMSHLHTFRATFQEPLYPALRLWEGAISIPRLP
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
6Phosphorylation--MAGAATGSRTPGR
--CCCCCCCCCCCCC
34.8527251275
8PhosphorylationMAGAATGSRTPGRSE
CCCCCCCCCCCCCHH
28.7324719451
10PhosphorylationGAATGSRTPGRSELV
CCCCCCCCCCCHHHC
31.6221712546
14PhosphorylationGSRTPGRSELVEGCG
CCCCCCCHHHCCCCC
40.9921712546
70UbiquitinationEAAVHVQKLSQECLK
HHHHHHHHHCHHHHH
49.36-
72PhosphorylationAVHVQKLSQECLKQL
HHHHHHHCHHHHHHH
30.8526074081
77UbiquitinationKLSQECLKQLAIKKQ
HHCHHHHHHHHHHHH
55.73-
83UbiquitinationLKQLAIKKQQHIDNI
HHHHHHHHHHHHHCC
49.42-
99UbiquitinationQIEDATEKLKANAES
HHHHHHHHHHHHHHH
51.43-
108UbiquitinationKANAESSKTWLKGKF
HHHHHHCCHHHHCCH
53.66-
114UbiquitinationSKTWLKGKFTELRLL
CCHHHHCCHHHHHHH
47.74-
130UbiquitinationDEEEALAKKFIDKNT
CHHHHHHHHHCCCCC
49.41-
131UbiquitinationEEEALAKKFIDKNTQ
HHHHHHHHHCCCCCC
41.78-
135UbiquitinationLAKKFIDKNTQLTLQ
HHHHHCCCCCCEEEH
58.01-
139 (in isoform 4)Phosphorylation-4.9324114839
232UbiquitinationTPLDIRLKESINCQL
CCCCCEEHHHHCCCC
39.30-
246UbiquitinationLSDPSSTKPGTLLKT
CCCCCCCCCCCEEEC
43.32-
252UbiquitinationTKPGTLLKTSPSPER
CCCCCEEECCCCHHH
50.50-
264UbiquitinationPERSLLLKYARTPTL
HHHHHHHHHCCCCCC
36.51-
365UbiquitinationNRQSWCLKRYDLEYW
CCCCHHCCCCCCEEE
45.86-
371PhosphorylationLKRYDLEYWAFHDGQ
CCCCCCEEEEEECCC
14.8820049867
437PhosphorylationRLWEGAISIPRLP--
HHHCCCCCCCCCC--
26.4624719451

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 TRI14_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI14_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 TRI14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAVS_HUMANMAVSphysical
24379373
NEMO_HUMANIKBKGphysical
24379373

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI14_HUMAN

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Related Literatures of Post-Translational Modification

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