DEDD_HUMAN - dbPTM
DEDD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEDD_HUMAN
UniProt AC O75618
Protein Name Death effector domain-containing protein
Gene Name DEDD
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Cytoplasm. Nucleus, nucleolus. Translocated to the nucleus during CD95-mediated apoptosis where it is localized in the nucleoli (By similarity). Following apoptosis induction, the mono and/or diubiquitination form increases and forms filamentous stru
Protein Description A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro (By similarity)..
Protein Sequence MAGLKRRASQVWPEEHGEQEHGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKRRRAVCPDLVDKYLEETSIRYVTPRALSDPEPRPPQPSKTVPPHYPVVCCPTSGPQMCSKRPARGRATLGSQRKRRKSVTPDPKEKQTCDIRLRVRAEYCQHETALQGNVFSNKQDPLERQFERFNQANTILKSRDLGSIICDIKFSELTYLDAFWRDYINGSLLEALKGVFITDSLKQAVGHEAIKLLVNVDEEDYELGRQKLLRNLMLQALP
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
9PhosphorylationAGLKRRASQVWPEEH
CCCCCHHHHCCCHHH
24.3729449344
25PhosphorylationEQEHGLYSLHRMFDI
CCCCCCHHHHHHHHH
23.8124719451
46PhosphorylationHRDVRVLSFLFVDVI
CCHHHHHHEEEEEEC
19.62-
116UbiquitinationVCPDLVDKYLEETSI
CCHHHHHHHHHHCCC
44.23-
181AcetylationGSQRKRRKSVTPDPK
CCHHHHHCCCCCCHH
54.0030588105
182PhosphorylationSQRKRRKSVTPDPKE
CHHHHHCCCCCCHHH
29.4328102081
184PhosphorylationRKRRKSVTPDPKEKQ
HHHHCCCCCCHHHCC
29.1228348404
237UbiquitinationNQANTILKSRDLGSI
HHHHHHHHHCCCCCE
39.332189047
237 (in isoform 1)Ubiquitination-39.3321890473
267 (in isoform 2)Ubiquitination-25.8721890473
282UbiquitinationVFITDSLKQAVGHEA
CCCCHHHHHHHCHHH
39.91-

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 DEDD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEDD_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 DEDD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RANB3_HUMANRANBP3physical
17353931
KHK_HUMANKHKphysical
17353931
TAP26_HUMANCCDC59physical
17353931
CASP8_HUMANCASP8physical
11965497
CFLAR_HUMANCFLARphysical
11965497
DEDD_HUMANDEDDphysical
12527898
DEDD2_HUMANDEDD2physical
12527898
DEDD_HUMANDEDDphysical
11965497
DEDD2_HUMANDEDD2physical
11965497
TF3C3_HUMANGTF3C3physical
11965497
A4_HUMANAPPphysical
21832049
GLYC_HUMANSHMT1physical
21988832
APLP2_HUMANAPLP2physical
20195357

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 DEDD_HUMAN

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Related Literatures of Post-Translational Modification

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