TNR8_HUMAN - dbPTM
TNR8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNR8_HUMAN
UniProt AC P28908
Protein Name Tumor necrosis factor receptor superfamily member 8 {ECO:0000312|HGNC:HGNC:11923}
Gene Name TNFRSF8 {ECO:0000312|HGNC:HGNC:11923}
Organism Homo sapiens (Human).
Sequence Length 595
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cytoplasm.
Protein Description Receptor for TNFSF8/CD30L. May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B..
Protein Sequence MRVLLAALGLLFLGALRAFPQDRPFEDTCHGNPSHYYDKAVRRCCYRCPMGLFPTQQCPQRPTDCRKQCEPDYYLDEADRCTACVTCSRDDLVEKTPCAWNSSRVCECRPGMFCSTSAVNSCARCFFHSVCPAGMIVKFPGTAQKNTVCEPASPGVSPACASPENCKEPSSGTIPQAKPTPVSPATSSASTMPVRGGTRLAQEAASKLTRAPDSPSSVGRPSSDPGLSPTQPCPEGSGDCRKQCEPDYYLDEAGRCTACVSCSRDDLVEKTPCAWNSSRTCECRPGMICATSATNSCARCVPYPICAAETVTKPQDMAEKDTTFEAPPLGTQPDCNPTPENGEAPASTSPTQSLLVDSQASKTLPIPTSAPVALSSTGKPVLDAGPVLFWVILVLVVVVGSSAFLLCHRRACRKRIRQKLHLCYPVQTSQPKLELVDSRPRRSSTQLRSGASVTEPVAEERGLMSQPLMETCHSVGAAYLESLPLQDASPAGGPSSPRDLPEPRVSTEHTNNKIEKIYIMKADTVIVGTVKAELPEGRGLAGPAEPELEEELEADHTPHYPEQETEPPLGSCSDVMLSVEEEGKEDPLPTAASGK
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
4 (in isoform 3)Phosphorylation-1.5827762562
32N-linked_GlycosylationFEDTCHGNPSHYYDK
CCCCCCCCHHHHHHH		15.96-
101N-linked_GlycosylationEKTPCAWNSSRVCEC
HHCCCCCCCCCCEEE		16.16UniProtKB CARBOHYD
153O-linked_GlycosylationNTVCEPASPGVSPAC
CCEECCCCCCCCCCC		32.66OGP
157O-linked_GlycosylationEPASPGVSPACASPE
CCCCCCCCCCCCCCC		16.82OGP
170O-linked_GlycosylationPENCKEPSSGTIPQA
CCCCCCCCCCCCCCC		42.35OGP
171O-linked_GlycosylationENCKEPSSGTIPQAK
CCCCCCCCCCCCCCC		51.15OGP
173O-linked_GlycosylationCKEPSSGTIPQAKPT
CCCCCCCCCCCCCCC		31.28OGP
186O-linked_GlycosylationPTPVSPATSSASTMP
CCCCCCCCCCCCCCC		26.97OGP
206O-linked_GlycosylationRLAQEAASKLTRAPD
HHHHHHHHHHCCCCC		34.9355829411
209PhosphorylationQEAASKLTRAPDSPS
HHHHHHHCCCCCCCH		28.6422210691
209O-linked_GlycosylationQEAASKLTRAPDSPS
HHHHHHHCCCCCCCH		28.6455829415
214PhosphorylationKLTRAPDSPSSVGRP
HHCCCCCCCHHCCCC		26.1421406692
214O-linked_GlycosylationKLTRAPDSPSSVGRP
HHCCCCCCCHHCCCC		26.14OGP
216PhosphorylationTRAPDSPSSVGRPSS
CCCCCCCHHCCCCCC		41.4221406692
217PhosphorylationRAPDSPSSVGRPSSD
CCCCCCHHCCCCCCC		31.7921406692
222O-linked_GlycosylationPSSVGRPSSDPGLSP
CHHCCCCCCCCCCCC		46.11OGP
230O-linked_GlycosylationSDPGLSPTQPCPEGS
CCCCCCCCCCCCCCC		41.59OGP
237PhosphorylationTQPCPEGSGDCRKQC
CCCCCCCCCCHHHHC		29.7822210691
276N-linked_GlycosylationEKTPCAWNSSRTCEC
HHCCCCCCCCCCCCC		16.16UniProtKB CARBOHYD
308UbiquitinationVPYPICAAETVTKPQ
CCCCCEEEEEECCCH		14.47-
312O-linked_GlycosylationICAAETVTKPQDMAE
CEEEEEECCCHHHCC		44.41OGP
333 (in isoform 3)Phosphorylation-48.2129485707
336N-linked_GlycosylationLGTQPDCNPTPENGE
CCCCCCCCCCCCCCC		51.35-
337 (in isoform 3)Phosphorylation-56.5129485707
340 (in isoform 3)Phosphorylation-79.1029485707
348O-linked_GlycosylationNGEAPASTSPTQSLL
CCCCCCCCCCCCCEE		40.61OGP
351O-linked_GlycosylationAPASTSPTQSLLVDS
CCCCCCCCCCEEECC		30.47OGP
419UbiquitinationCRKRIRQKLHLCYPV
HHHHHHHHHCCCCCC		28.20-
428PhosphorylationHLCYPVQTSQPKLEL
CCCCCCCCCCCCEEE		29.5730108239
429PhosphorylationLCYPVQTSQPKLELV
CCCCCCCCCCCEEEC		27.6530108239
438PhosphorylationPKLELVDSRPRRSST
CCEEECCCCCCCCCC		36.3830108239
443PhosphorylationVDSRPRRSSTQLRSG
CCCCCCCCCCCCCCC		38.7326074081
444PhosphorylationDSRPRRSSTQLRSGA
CCCCCCCCCCCCCCC		20.5426074081
445PhosphorylationSRPRRSSTQLRSGAS
CCCCCCCCCCCCCCC		32.6326074081
449PhosphorylationRSSTQLRSGASVTEP
CCCCCCCCCCCCCCC		47.5025262027
452PhosphorylationTQLRSGASVTEPVAE
CCCCCCCCCCCCHHH		32.8523401153
454PhosphorylationLRSGASVTEPVAEER
CCCCCCCCCCHHHHC		31.8826074081
479PhosphorylationCHSVGAAYLESLPLQ
HHHHCHHHHHCCCCC		15.5220090780
482PhosphorylationVGAAYLESLPLQDAS
HCHHHHHCCCCCCCC		32.4626074081
489PhosphorylationSLPLQDASPAGGPSS
CCCCCCCCCCCCCCC		24.4626074081
495PhosphorylationASPAGGPSSPRDLPE
CCCCCCCCCCCCCCC		57.1426074081
496PhosphorylationSPAGGPSSPRDLPEP
CCCCCCCCCCCCCCC		27.3926074081
506PhosphorylationDLPEPRVSTEHTNNK
CCCCCCCCCCCCCCC		29.3826074081
507PhosphorylationLPEPRVSTEHTNNKI
CCCCCCCCCCCCCCE		29.0026074081
510PhosphorylationPRVSTEHTNNKIEKI
CCCCCCCCCCCEEEE		33.9626074081
518PhosphorylationNNKIEKIYIMKADTV
CCCEEEEEEEECCEE		13.1619581576
524PhosphorylationIYIMKADTVIVGTVK
EEEEECCEEEEEEEE		19.5929978859
560PhosphorylationEADHTPHYPEQETEP
HCCCCCCCCCCCCCC		15.07-
593PhosphorylationDPLPTAASGK-----
CCCCCCCCCC-----		44.6522985185
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 TNR8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNR8_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 TNR8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYDP2_HUMANTDP2physical
10764746
TRAF5_HUMANTRAF5physical
8999898
TRAF2_HUMANTRAF2physical
8999898
TRAIP_HUMANTRAIPphysical
9104814
TRAF1_HUMANTRAF1physical
8662842
TRAF2_HUMANTRAF2physical
8662842
TRAF3_HUMANTRAF3physical
8662842
TRAF5_HUMANTRAF5physical
9511754
TRAF1_HUMANTRAF1physical
9168896
TRAF2_HUMANTRAF2physical
9168896
TRAF3_HUMANTRAF3physical
9168896
TRAF1_MOUSETraf1physical
8627180
TRAF2_MOUSETraf2physical
8627180
TNR8_HUMANTNFRSF8physical
11971184
TRAF2_HUMANTRAF2physical
11971184
NAA25_HUMANNAA25physical
28514442
CC112_HUMANCCDC112physical
28514442
NAA20_HUMANNAA20physical
28514442
CEP57_HUMANCEP57physical
28514442
TRAF3_HUMANTRAF3physical
28514442
D19L1_HUMANDPY19L1physical
28514442
DAPK3_HUMANDAPK3physical
28514442
TRAF1_HUMANTRAF1physical
28514442
SPAS2_HUMANSPATS2physical
28514442
BL1S1_HUMANBLOC1S1physical
28514442
TRAF2_HUMANTRAF2physical
28514442
EXOC1_HUMANEXOC1physical
28514442
VATD_HUMANATP6V1Dphysical
28514442
GLP3L_HUMANGOLPH3Lphysical
28514442
RGAP1_HUMANRACGAP1physical
28514442
FHL2_HUMANFHL2physical
28514442
KIF3A_HUMANKIF3Aphysical
28514442
NDC1_HUMANNDC1physical
28514442
CDC6_HUMANCDC6physical
28514442
GOLP3_HUMANGOLPH3physical
28514442
Drug and Disease Associations
Kegg Disease
H00007 Hodgkin lymphoma
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D04612 Iratumumab (USAN)
D09587 Brentuximab vedotin (genetical recombination) (JAN); Brentuximab vedotin (USAN); Adcetris (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNR8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND MASSSPECTROMETRY.

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