DDIT3_HUMAN - dbPTM
DDIT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDIT3_HUMAN
UniProt AC P35638
Protein Name DNA damage-inducible transcript 3 protein
Gene Name DDIT3
Organism Homo sapiens (Human).
Sequence Length 169
Subcellular Localization Cytoplasm. Nucleus. Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation.
Protein Description Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response..
Protein Sequence MAAESLPFSFGTLSSWELEAWYEDLQEVLSSDENGGTYVSPPGNEEEESKIFTTLDPASLAWLTEEEPEPAEVTSTSQSPHSPDSSQSSLAQEEEEEDQGRTRKRKQSGHSPARAGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRRALIDRMVNLHQA
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
14PhosphorylationPFSFGTLSSWELEAW
CCCCCCCCCHHHHHH
32.9922817900
15PhosphorylationFSFGTLSSWELEAWY
CCCCCCCCHHHHHHH
27.9022817900
30PhosphorylationEDLQEVLSSDENGGT
HHHHHHHHCCCCCCE
40.7022817900
31PhosphorylationDLQEVLSSDENGGTY
HHHHHHHCCCCCCEE
44.7922817900
49PhosphorylationPGNEEEESKIFTTLD
CCCHHHHHCCEECCC
34.04-
54PhosphorylationEESKIFTTLDPASLA
HHHCCEECCCHHHHH
20.58-
64PhosphorylationPASLAWLTEEEPEPA
HHHHHHHCCCCCCCC
30.56-
77PhosphorylationPAEVTSTSQSPHSPD
CCCCCCCCCCCCCCC
28.5522468782
79PhosphorylationEVTSTSQSPHSPDSS
CCCCCCCCCCCCCCC
25.098650547
82PhosphorylationSTSQSPHSPDSSQSS
CCCCCCCCCCCCCCH
33.518650547
88PhosphorylationHSPDSSQSSLAQEEE
CCCCCCCCHHHHHHH
29.3022468782

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
14SPhosphorylationKinaseCSNK2A1P68400
GPS
14SPhosphorylationKinaseCK2-FAMILY-GPS
14SPhosphorylationKinaseCK2_GROUP-PhosphoELM
14SPhosphorylationKinaseCK2-Uniprot
15SPhosphorylationKinaseCSNK2A1P68400
GPS
15SPhosphorylationKinaseCK2_GROUP-PhosphoELM
15SPhosphorylationKinaseCK2-FAMILY-GPS
15SPhosphorylationKinaseCK2-Uniprot
30SPhosphorylationKinasePRKAA1Q13131
GPS
30SPhosphorylationKinaseCSNK2A1P68400
GPS
30SPhosphorylationKinaseCK2_GROUP-PhosphoELM
30SPhosphorylationKinaseCK2-FAMILY-GPS
30SPhosphorylationKinaseCK2-Uniprot
31SPhosphorylationKinaseCK2_GROUP-PhosphoELM
31SPhosphorylationKinaseCK2-Uniprot
31SPhosphorylationKinaseCK2-FAMILY-GPS
31SPhosphorylationKinaseCSNK2A1P68400
GPS
79SPhosphorylationKinaseP38-SUBFAMILY-GPS
79SPhosphorylationKinaseP38_GROUP-PhosphoELM
79SPhosphorylationKinaseP38AQ16539
PSP
82SPhosphorylationKinaseP38-SUBFAMILY-GPS
82SPhosphorylationKinaseP38_GROUP-PhosphoELM
82SPhosphorylationKinaseP38AQ16539
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDIT3_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 DDIT3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHB14_HUMANHSD17B14physical
16189514
MCMBP_HUMANMCMBPphysical
16189514
SPOP_HUMANSPOPphysical
16189514
BATF_HUMANBATFphysical
16189514
CSK21_HUMANCSNK2A1physical
12876286
CEBPB_HUMANCEBPBphysical
12706815
CEBPB_HUMANCEBPBphysical
8662954
JUND_HUMANJUNDphysical
10523647
FOS_HUMANFOSphysical
10523647
JUN_HUMANJUNphysical
10523647
ATF3_HUMANATF3physical
8622660
CN080_HUMANC14orf80physical
20562859
RTL6_HUMANLDOC1Lphysical
20562859
CEBPB_HUMANCEBPBphysical
20562859
HXA5_HUMANHOXA5physical
20211142
SSX3_HUMANSSX3physical
20211142
RAI1_HUMANRAI1physical
20211142
ZSC31_HUMANZSCAN31physical
20211142
HDAC1_HUMANHDAC1physical
22242125
SRA1_HUMANSRA1physical
20398657
CSN8_HUMANCOPS8physical
23213463
CUL3_HUMANCUL3physical
23213463
CUL1_HUMANCUL1physical
23213463
CSN3_HUMANCOPS3physical
23213463
KEAP1_HUMANKEAP1physical
23213463
BACH2_HUMANBACH2physical
23661758
BACH1_HUMANBACH1physical
23661758
MAFG_HUMANMAFGphysical
23661758
MAFF_HUMANMAFFphysical
23661758
BATF3_HUMANBATF3physical
23661758
BATF2_HUMANBATF2physical
23661758
BATF_HUMANBATFphysical
23661758
ATF3_HUMANATF3physical
23661758
ATF4_HUMANATF4physical
23661758
FOSL1_HUMANFOSL1physical
23661758
FOS_HUMANFOSphysical
23661758
JUNB_HUMANJUNBphysical
23661758
JUN_HUMANJUNphysical
23661758
ATF2_HUMANATF2physical
23661758
EPAS1_HUMANEPAS1physical
23661758
DBP_HUMANDBPphysical
23661758
NFIL3_HUMANNFIL3physical
23661758
CR3L1_HUMANCREB3L1physical
23661758
CREB3_HUMANCREB3physical
23661758
DDIT3_HUMANDDIT3physical
23661758
THRB_HUMANF2physical
21988832
GP1BA_HUMANGP1BAphysical
21988832
IMA1_HUMANKPNA2physical
21988832
NEMO_HUMANIKBKGphysical
21988832
IDD_HUMANDGCR2physical
21988832
PPIB_HUMANPPIBphysical
24270407
ATF4_HUMANATF4physical
18330356
BATF_HUMANBATFphysical
18330356
CN080_HUMANC14orf80physical
18330356
GIPC1_HUMANGIPC1physical
18330356
EP300_HUMANEP300physical
17872950
TRIB3_HUMANTRIB3physical
17872950
FOSL2_HUMANFOSL2physical
25416956
RBTN2_HUMANLMO2physical
25416956
ZBT25_HUMANZBTB25physical
25416956
TNF12_HUMANTNFSF12physical
25416956
SNPC5_HUMANSNAPC5physical
25416956
DHB14_HUMANHSD17B14physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
BATF3_HUMANBATF3physical
25416956
EMSY_HUMANC11orf30physical
25416956
ZC3HE_HUMANZC3H14physical
25416956
ATPF2_HUMANATPAF2physical
25416956
CC153_HUMANCCDC153physical
25416956
CBP_HUMANCREBBPphysical
20829347
CEBPB_HUMANCEBPBphysical
1547942
SPOP_HUMANSPOPphysical
24990631
GABR2_HUMANGABBR2physical
16081421
CEBPA_HUMANCEBPAphysical
27555288
FANCA_HUMANFANCAphysical
28215707
PRKN_HUMANPARK2physical
28522833

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613488Myxoid liposarcoma (MXLIPO)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDIT3_HUMAN

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Related Literatures of Post-Translational Modification

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