TRADD_HUMAN - dbPTM
TRADD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRADD_HUMAN
UniProt AC Q15628
Protein Name Tumor necrosis factor receptor type 1-associated DEATH domain protein
Gene Name TRADD
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Nucleus. Cytoplasm. Cytoplasm, cytoskeleton . Shuttles between the cytoplasm and the nucleus..
Protein Description The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B..
Protein Sequence MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQMLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRAGAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGARGGDGEVASAPLQPPVPSLSEVKPPPPPPPAQTFLFQGQPVVNRPLSLKDQQTFARSVGLKWRKVGRSLQRGCRALRDPALDSLAYEYEREGLYEQAFQLLRRFVQAEGRRATLQRLVEALEENELTSLAEDLLGLTDPNGGLA
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
32PhosphorylationKVVLSDAYAHPQQKV
EEHHHCCCCCHHHHH
15.5027642862
38UbiquitinationAYAHPQQKVAVYRAL
CCCCHHHHHHHHHHH
27.2429967540
42PhosphorylationPQQKVAVYRALQAAL
HHHHHHHHHHHHHHH
4.76-
102PhosphorylationLRAALQRSLAAALAQ
HHHHHHHHHHHHHHH
14.9220068231
103UbiquitinationRAALQRSLAAALAQH
HHHHHHHHHHHHHHC
4.0222817900
103UbiquitinationRAALQRSLAAALAQH
HHHHHHHHHHHHHHC
4.02-
111PhosphorylationAAALAQHSVPLQLEL
HHHHHHCCCCEEEEH
17.2220068231
137PhosphorylationADEERCLSCILAQQP
CCHHHHHHHHHHCCC
11.6128857561
163UbiquitinationEDALRNLKCGSGARG
HHHHHHCCCCCCCCC
39.8522817900
169UbiquitinationLKCGSGARGGDGEVA
CCCCCCCCCCCCCCC
53.83-
215PhosphorylationPVVNRPLSLKDQQTF
ECCCCCCCHHCHHHH
35.7421724995
229UbiquitinationFARSVGLKWRKVGRS
HHHHHCCHHHHHHHH
38.74-
254PhosphorylationPALDSLAYEYEREGL
HHHHHHHHHHHHCCH
25.0828796482
256PhosphorylationLDSLAYEYEREGLYE
HHHHHHHHHHCCHHH
13.9628796482
296PhosphorylationLEENELTSLAEDLLG
HHHCCCHHHHHHHHC
37.9021724995

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 TRADD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRADD_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 TRADD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
14743216
STAT1_HUMANSTAT1physical
10848577
TRAF2_HUMANTRAF2physical
10892748
TRAF2_HUMANTRAF2physical
10911999
NOL3_HUMANNOL3genetic
9560245
RIPK1_HUMANRIPK1physical
8612133
TNR1A_HUMANTNFRSF1Aphysical
8565075
TRAF2_HUMANTRAF2physical
8565075
FADD_HUMANFADDphysical
8565075
TRADD_HUMANTRADDphysical
8943045
TRAF2_HUMANTRAF2physical
9020361
K1C18_HUMANKRT18physical
11684708
RIPK1_HUMANRIPK1physical
16603398
SH3K1_HUMANSH3KBP1physical
15707590
TRIPC_HUMANTRIP12physical
22561347
FADD_HUMANFADDphysical
21724995
RIPK1_HUMANRIPK1physical
21724995
TRADD_HUMANTRADDphysical
7758105
TRAF2_HUMANTRAF2physical
12796506
DAB2P_HUMANDAB2IPphysical
15310755
ZMY11_HUMANZMYND11physical
19379743
RIPK1_HUMANRIPK1physical
24735611
IFIT3_HUMANIFIT3physical
21813773
TRAF6_HUMANTRAF6physical
24758719

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 TRADD_HUMAN

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Related Literatures of Post-Translational Modification

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