TRIB3_HUMAN - dbPTM
TRIB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIB3_HUMAN
UniProt AC Q96RU7
Protein Name Tribbles homolog 3
Gene Name TRIB3
Organism Homo sapiens (Human).
Sequence Length 358
Subcellular Localization Nucleus .
Protein Description Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1. Binds to ATF4 and inhibits its transcriptional activation activity. Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. Interacts with MAPK kinases and regulates activation of MAP kinases. May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. Does not display kinase activity. Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress. Can inhibit APOBEC3A editing of nuclear DNA..
Protein Sequence MRATPLAAPAGSLSRKKRLELDDNLDTERPVQKRARSGPQPRLPPCLLPLSPPTAPDRATAVATASRLGPYVLLEPEEGGRAYQALHCPTGTEYTCKVYPVQEALAVLEPYARLPPHKHVARPTEVLAGTQLLYAFFTRTHGDMHSLVRSRHRIPEPEAAVLFRQMATALAHCHQHGLVLRDLKLCRFVFADRERKKLVLENLEDSCVLTGPDDSLWDKHACPAYVGPEILSSRASYSGKAADVWSLGVALFTMLAGHYPFQDSEPVLLFGKIRRGAYALPAGLSAPARCLVRCLLRREPAERLTATGILLHPWLRQDPMPLAPTRSHLWEAAQVVPDGLGLDEAREEEGDREVVLYG
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
4Phosphorylation----MRATPLAAPAG
----CCCCCCCCCCC
14.4224719451
12PhosphorylationPLAAPAGSLSRKKRL
CCCCCCCCCCCCCCC
25.8526434776
14PhosphorylationAAPAGSLSRKKRLEL
CCCCCCCCCCCCCCC
43.6926434776
33UbiquitinationDTERPVQKRARSGPQ
CCCCCHHHHHHCCCC
48.54-
37PhosphorylationPVQKRARSGPQPRLP
CHHHHHHCCCCCCCC
54.5724706070
39PhosphorylationQKRARSGPQPRLPPC
HHHHHCCCCCCCCCC
42.10-
41PhosphorylationRARSGPQPRLPPCLL
HHHCCCCCCCCCCCC
42.80-
44UbiquitinationSGPQPRLPPCLLPLS
CCCCCCCCCCCCCCC
20.88-
51PhosphorylationPPCLLPLSPPTAPDR
CCCCCCCCCCCCCCH
27.2223312004
54PhosphorylationLLPLSPPTAPDRATA
CCCCCCCCCCCHHHH
54.9623312004
60UbiquitinationPTAPDRATAVATASR
CCCCCHHHHHHHHHH
23.66-
64PhosphorylationDRATAVATASRLGPY
CHHHHHHHHHHHCCE
20.68-
78PhosphorylationYVLLEPEEGGRAYQA
EEEECCCCCCCEEEE
77.11-
97UbiquitinationTGTEYTCKVYPVQEA
CCCEEEEEEEEHHHH
36.68-
124UbiquitinationHKHVARPTEVLAGTQ
CCCCCCCHHHHHHHH
32.92-
215PhosphorylationVLTGPDDSLWDKHAC
EEECCCCCCCCCCCC
38.45-
224UbiquitinationWDKHACPAYVGPEIL
CCCCCCCCHHCHHHH
16.13-
232PhosphorylationYVGPEILSSRASYSG
HHCHHHHCCCCCCCC
24.3624719451
233PhosphorylationVGPEILSSRASYSGK
HCHHHHCCCCCCCCC
28.5524719451
246UbiquitinationGKAADVWSLGVALFT
CCHHHHHHHHHHHHH
18.33-

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 ligaseSIAH1Q8IUQ4
PMID:18276110

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIB3_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 TRIB3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATF4_HUMANATF4physical
12743605
AKT1_HUMANAKT1physical
12791994
TF65_HUMANRELAphysical
12736262
CSN6_HUMANCOPS6physical
16169070
GDF9_HUMANGDF9physical
16169070
GIT1_HUMANGIT1physical
16169070
SETB1_HUMANSETDB1physical
16169070
RBM48_HUMANRBM48physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
KAT5_HUMANKAT5physical
16169070
ATF4_HUMANATF4physical
18276110
ATF5_HUMANATF5physical
18276110
CSK2B_HUMANCSNK2Bphysical
18276110
FINC_HUMANFN1physical
18276110
GRN_HUMANGRNphysical
18276110
1B07_HUMANHLA-Bphysical
18276110
1B18_HUMANHLA-Bphysical
18276110
LTBP4_HUMANLTBP4physical
18276110
GANP_HUMANMCM3APphysical
18276110
SIAH1_HUMANSIAH1physical
18276110
RIDA_HUMANHRSP12physical
18276110
PSA3_HUMANPSMA3physical
18276110
RBM4_HUMANRBM4physical
18276110
RSSA_HUMANRPSAphysical
18276110
TIAF1_HUMANTIAF1physical
18276110
SMAD3_HUMANSMAD3physical
21896644
SMUF1_HUMANSMURF1physical
17576816
A4_HUMANAPPphysical
21832049
ANM5_HUMANPRMT5physical
23455924
STK40_HUMANSTK40physical
26186194
GALD1_HUMANPDDC1physical
26186194
RFWD2_HUMANRFWD2physical
26186194
SQSTM_HUMANSQSTM1physical
26268733
STK40_HUMANSTK40physical
28514442
RFWD2_HUMANRFWD2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIB3_HUMAN

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Related Literatures of Post-Translational Modification

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