TR10A_HUMAN - dbPTM
TR10A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TR10A_HUMAN
UniProt AC O00220
Protein Name Tumor necrosis factor receptor superfamily member 10A
Gene Name TNFRSF10A
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Receptor for the cytotoxic ligand TNFSF10/TRAIL. [PubMed: 26457518 The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.]
Protein Sequence MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE
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
36UbiquitinationAAAATPSKVWGSSAG
CCCCCCCHHCCCCCC
43.1221906983
52MethylationIEPRGGGRGALPTSM
CCCCCCCCCCCCCCC
30.4124129315
57O-linked_GlycosylationGGRGALPTSMGQHGP
CCCCCCCCCCCCCCH
31.99OGP
83PhosphorylationPRPAREASPRLRVHK
CCCCCCCCCCCCCCC
13.0522817900
126O-linked_GlycosylationGTQQWEHSPLGELCP
CCCCCCCCCCCCCCC
15.42OGP
156N-linked_GlycosylationTEGVGYTNASNNLFA
CCCCCCCCCCCCEEE
32.65UniProtKB CARBOHYD
178PhosphorylationKSDEEERSPCTTTRN
CCCHHHCCCCCCCCC
27.8325159151
191UbiquitinationRNTACQCKPGTFRND
CCCCCCCCCCCCCCC
22.1721963094
217UbiquitinationGCPRGMVKVKDCTPW
CCCCCCEECCCCCCH
34.3727667366
219UbiquitinationPRGMVKVKDCTPWSD
CCCCEECCCCCCHHH
41.1729967540
261S-palmitoylationLVAVLIVCCCIGSGC
HHHHHHHHHHHCCCC
0.9319090789
262S-palmitoylationVAVLIVCCCIGSGCG
HHHHHHHHHHCCCCC
1.0019090789
263S-palmitoylationAVLIVCCCIGSGCGG
HHHHHHHHHCCCCCC
3.1419090789
273UbiquitinationSGCGGDPKCMDRVCF
CCCCCCHHHHHHHHH
47.10-
336S-nitrosylationQSPGEAQCLLGPAEA
CCCCCEEEEECCCCC
4.3422178444
336S-nitrosocysteineQSPGEAQCLLGPAEA
CCCCCEEEEECCCCC
4.34-
379PhosphorylationANIVPFDSWDQLMRQ
CCCCCCCCHHHHHHH
32.6922210691
390PhosphorylationLMRQLDLTKNEIDVV
HHHHHCCCCCCCCEE
31.3322210691
391UbiquitinationMRQLDLTKNEIDVVR
HHHHCCCCCCCCEEE
60.9421906983
424PhosphorylationNKTGRNASIHTLLDA
HHHCCCCHHHHHHHH
20.6022617229
424O-linked_GlycosylationNKTGRNASIHTLLDA
HHHCCCCHHHHHHHH
20.6030987996
427PhosphorylationGRNASIHTLLDALER
CCCCHHHHHHHHHHH
27.6120873877
443UbiquitinationEERHAREKIQDLLVD
HHHHHHHHHHHHHHH
39.8621906983
453UbiquitinationDLLVDSGKFIYLEDG
HHHHHCCCEEEEECC
32.3229967540
456PhosphorylationVDSGKFIYLEDGTGS
HHCCCEEEEECCCCC
13.7425884760
461PhosphorylationFIYLEDGTGSAVSLE
EEEEECCCCCCEECC
40.0428176443
463PhosphorylationYLEDGTGSAVSLE--
EEECCCCCCEECC--
25.9026503892
466PhosphorylationDGTGSAVSLE-----
CCCCCCEECC-----
26.8826503892

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 ligaseMARCHF5Q9NX47
PMID:23300075

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TR10A_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 TR10A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL10_HUMANBCL10physical
10400625
CASP8_HUMANCASP8physical
9325248
CASPA_HUMANCASP10physical
9325248
CFLAR_HUMANCFLARphysical
9325248
RT29_HUMANDAP3physical
11376335
TRADD_HUMANTRADDphysical
9430227
FADD_HUMANFADDphysical
9430227
TNF10_HUMANTNFSF10physical
9082980
CBL_HUMANCBLphysical
19932172
CFLAR_HUMANCFLARphysical
19343040
CASP8_HUMANCASP8physical
19343040
FADD_HUMANFADDphysical
15280356
CASP8_HUMANCASP8physical
15280356
CASP8_HUMANCASP8physical
15388581
FADD_HUMANFADDphysical
15388581
TR10B_HUMANTNFRSF10Bphysical
15388581
SQSTM_HUMANSQSTM1physical
19427028
CASP8_HUMANCASP8physical
19427028
TR10B_HUMANTNFRSF10Bphysical
19427028
CASP8_HUMANCASP8physical
23142077
CFLAR_HUMANCFLARphysical
23142077
FADD_HUMANFADDphysical
23142077
TRAF2_HUMANTRAF2physical
23142077
CUL3_HUMANCUL3physical
23142077
MARH1_HUMANMARCH1physical
23300075
MARH8_HUMANMARCH8physical
23300075
CFLAR_HUMANCFLARphysical
27321185
FADD_HUMANFADDphysical
27321185
CASP8_HUMANCASP8physical
27321185
CASP8_HUMANCASP8physical
28514442
AL3B1_HUMANALDH3B1physical
28514442
FADD_HUMANFADDphysical
28514442
FGFR4_HUMANFGFR4physical
28514442
ERG7_HUMANLSSphysical
28514442
ACVR1_HUMANACVR1physical
28514442
CEGT_HUMANUGCGphysical
28514442
INAR1_HUMANIFNAR1physical
28514442
TR10B_HUMANTNFRSF10Bphysical
28514442
KCNT2_HUMANKCNT2physical
28514442
TMM94_HUMANKIAA0195physical
28514442
FBX11_HUMANFBXO11physical
28514442
LAP4B_HUMANLAPTM4Bphysical
28514442
S12A4_HUMANSLC12A4physical
28514442
ABCD4_HUMANABCD4physical
28514442
MP3B2_HUMANMAP1LC3B2physical
28514442
LRP10_HUMANLRP10physical
28514442
CARME_HUMANC9orf41physical
28514442
ST7L_HUMANST7Lphysical
28514442
RN149_HUMANRNF149physical
28514442
BT2A2_HUMANBTN2A2physical
28514442
CDC6_HUMANCDC6physical
28514442
ATG9A_HUMANATG9Aphysical
28514442
UBB_HUMANUBBphysical
28514442
ERMP1_HUMANERMP1physical
28514442
S10AA_HUMANS100A10physical
28514442
P4K2A_HUMANPI4K2Aphysical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
CD320_HUMANCD320physical
28514442
MFAP3_HUMANMFAP3physical
28514442
IL4RA_HUMANIL4Rphysical
28514442
DDRGK_HUMANDDRGK1physical
28514442
AVR2A_HUMANACVR2Aphysical
28514442
SDCB1_HUMANSDCBPphysical
28514442

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
D04858 Mapatumumab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TR10A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-463 AND SER-466,AND MASS SPECTROMETRY.

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