DDIT4_HUMAN - dbPTM
DDIT4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDIT4_HUMAN
UniProt AC Q9NX09
Protein Name DNA damage-inducible transcript 4 protein
Gene Name DDIT4
Organism Homo sapiens (Human).
Sequence Length 232
Subcellular Localization Mitochondrion. Cytoplasm, cytosol .
Protein Description Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes (By similarity). Required for mTORC1-mediated defense against viral protein synthesis and virus replication (By similarity). Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death..
Protein Sequence MPSLWDRFSSSSTSSSPSSLPRTPTPDRPPRSAWGSATREEGFDRSTSLESSDCESLDSSNSGFGPEEDTAYLDGVSLPDFELLSDPEDEHLCANLMQLLQESLAQARLGSRRPARLLMPSQLVSQVGKELLRLAYSEPCGLRGALLDVCVEQGKSCHSVGQLALDPSLVPTFQLTLVLRLDSRLWPKIQGLFSSANSPFLPGFSQSLTLSTGFRVIKKKLYSSEQLLIEEC
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
3Phosphorylation-----MPSLWDRFSS
-----CCCHHHHCCC
40.5721955146
9PhosphorylationPSLWDRFSSSSTSSS
CCHHHHCCCCCCCCC
30.1521955146
10PhosphorylationSLWDRFSSSSTSSSP
CHHHHCCCCCCCCCC
26.1221955146
11PhosphorylationLWDRFSSSSTSSSPS
HHHHCCCCCCCCCCC
36.1221955146
12PhosphorylationWDRFSSSSTSSSPSS
HHHCCCCCCCCCCCC
33.9721955146
13PhosphorylationDRFSSSSTSSSPSSL
HHCCCCCCCCCCCCC
34.2821955146
14PhosphorylationRFSSSSTSSSPSSLP
HCCCCCCCCCCCCCC
30.6621955146
15PhosphorylationFSSSSTSSSPSSLPR
CCCCCCCCCCCCCCC
46.4821955146
16PhosphorylationSSSSTSSSPSSLPRT
CCCCCCCCCCCCCCC
28.6821955146
18PhosphorylationSSTSSSPSSLPRTPT
CCCCCCCCCCCCCCC
46.5921955146
19PhosphorylationSTSSSPSSLPRTPTP
CCCCCCCCCCCCCCC
45.8621955146
23PhosphorylationSPSSLPRTPTPDRPP
CCCCCCCCCCCCCCC
29.5824114839
25PhosphorylationSSLPRTPTPDRPPRS
CCCCCCCCCCCCCCC
36.8924114839
121PhosphorylationPARLLMPSQLVSQVG
CHHHHCHHHHHHHHH
23.3720166753
129UbiquitinationQLVSQVGKELLRLAY
HHHHHHHHHHHHHHH
46.4621906983
188UbiquitinationLDSRLWPKIQGLFSS
CCCCHHHHHHHHHHC
35.7621906983
218UbiquitinationSTGFRVIKKKLYSSE
HCCCHHHHHHCCCCC
40.78-
219UbiquitinationTGFRVIKKKLYSSEQ
CCCHHHHHHCCCCCH
36.57-
220UbiquitinationGFRVIKKKLYSSEQL
CCHHHHHHCCCCCHH
47.88-

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 ligasePRKNO60260
PMID:25101677
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:19557001
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:31406304

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDIT4_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 DDIT4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRIF1_HUMANLRIF1physical
16169070
CUL4A_HUMANCUL4Aphysical
19557001
DDB1_HUMANDDB1physical
19557001
FBW1A_HUMANBTRCphysical
19557001
PRKN_HUMANPARK2physical
25101677
HUWE1_HUMANHUWE1physical
25147182
NEDD4_HUMANNEDD4physical
27494837

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 DDIT4_HUMAN

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Related Literatures of Post-Translational Modification

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