TRAD1_HUMAN - dbPTM
TRAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRAD1_HUMAN
UniProt AC O14545
Protein Name TRAF-type zinc finger domain-containing protein 1
Gene Name TRAFD1
Organism Homo sapiens (Human).
Sequence Length 582
Subcellular Localization
Protein Description Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity)..
Protein Sequence MAEFLDDQETRLCDNCKKEIPVFNFTIHEIHCQRNIGMCPTCKEPFPKSDMETHMAAEHCQVTCKCNKKLEKRLLKKHEETECPLRLAVCQHCDLELSILKLKEHEDYCGARTELCGNCGRNVLVKDLKTHPEVCGREGEEKRNEVAIPPNAYDESWGQDGIWIASQLLRQIEALDPPMRLPRRPLRAFESDVFHNRTTNQRNITAQVSIQNNLFEEQERQERNRGQQPPKEGGEESANLDFMLALSLQNEGQASSVAEQDFWRAVCEADQSHGGPRSLSDIKGAADEIMLPCEFCEELYPEELLIDHQTSCNPSRALPSLNTGSSSPRGVEEPDVIFQNFLQQAASNQLDSLMGLSNSHPVEESIIIPCEFCGVQLEEEVLFHHQDQCDQRPATATNHVTEGIPRLDSQPQETSPELPRRRVRHQGDLSSGYLDDTKQETANGPTSCLPPSRPINNMTATYNQLSRSTSGPRPGCQPSSPCVPKLSNSDSQDIQGRNRDSQNGAIAPGHVSVIRPPQNLYPENIVPSFSPGPSGRYGASGRSEGGRNSRVTPAAANYRSRTAKAKPSKQQGAGDAEEEEEE
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
2Acetylation------MAEFLDDQE
------CCCCCCHHH		19.0922814378
172-HydroxyisobutyrylationTRLCDNCKKEIPVFN
HHCCCCCCCCCCEEE		60.75-
43UbiquitinationIGMCPTCKEPFPKSD
CCCCCCCCCCCCCCH		71.54-
43UbiquitinationIGMCPTCKEPFPKSD
CCCCCCCCCCCCCCH		71.54-
49PhosphorylationCKEPFPKSDMETHMA
CCCCCCCCHHHHHHH		42.2926657352
65UbiquitinationEHCQVTCKCNKKLEK
HHCCEEHHCCHHHHH		31.32-
65UbiquitinationEHCQVTCKCNKKLEK
HHCCEEHHCCHHHHH		31.32-
77AcetylationLEKRLLKKHEETECP
HHHHHHHHCCCCCCH		57.1027452117
77UbiquitinationLEKRLLKKHEETECP
HHHHHHHHCCCCCCH		57.10-
77UbiquitinationLEKRLLKKHEETECP
HHHHHHHHCCCCCCH		57.10-
98PhosphorylationQHCDLELSILKLKEH
HHCCCEEEEEEHHHC		19.2525159151
101UbiquitinationDLELSILKLKEHEDY
CCEEEEEEHHHCCCC		56.71-
103AcetylationELSILKLKEHEDYCG
EEEEEEHHHCCCCCC		56.2727452117
103UbiquitinationELSILKLKEHEDYCG
EEEEEEHHHCCCCCC		56.2721906983
103UbiquitinationELSILKLKEHEDYCG
EEEEEEHHHCCCCCC		56.2721890473
108PhosphorylationKLKEHEDYCGARTEL
EHHHCCCCCCCCCCC		6.9825839225
126UbiquitinationCGRNVLVKDLKTHPE
CCCCEEHHHHHCCHH		53.86-
126UbiquitinationCGRNVLVKDLKTHPE
CCCCEEHHHHHCCHH		53.86-
129UbiquitinationNVLVKDLKTHPEVCG
CEEHHHHHCCHHHHC		55.7221890473
142UbiquitinationCGREGEEKRNEVAIP
HCCCCCCCCCCCCCC		57.11-
191PhosphorylationRPLRAFESDVFHNRT
CCCCHHHCCCCCCCC		32.4020873877
198PhosphorylationSDVFHNRTTNQRNIT
CCCCCCCCCCCCCEE		35.1028555341
209PhosphorylationRNITAQVSIQNNLFE
CCEEEEEEEECCCHH		13.3322912867
272PhosphorylationAVCEADQSHGGPRSL
HHHHHHHHCCCCCCH		25.3325262027
278O-linked_GlycosylationQSHGGPRSLSDIKGA
HHCCCCCCHHHHCCC		35.0430379171
278PhosphorylationQSHGGPRSLSDIKGA
HHCCCCCCHHHHCCC		35.0423401153
280PhosphorylationHGGPRSLSDIKGAAD
CCCCCCHHHHCCCCC		38.2425159151
283UbiquitinationPRSLSDIKGAADEIM
CCCHHHHCCCCCCCC		47.70-
320PhosphorylationNPSRALPSLNTGSSS
CHHHCCCCCCCCCCC		34.7922167270
323PhosphorylationRALPSLNTGSSSPRG
HCCCCCCCCCCCCCC		43.6722167270
325PhosphorylationLPSLNTGSSSPRGVE
CCCCCCCCCCCCCCC		26.1329255136
326O-linked_GlycosylationPSLNTGSSSPRGVEE
CCCCCCCCCCCCCCC		45.7830379171
326PhosphorylationPSLNTGSSSPRGVEE
CCCCCCCCCCCCCCC		45.7829255136
327PhosphorylationSLNTGSSSPRGVEEP
CCCCCCCCCCCCCCC		21.9519664994
409PhosphorylationEGIPRLDSQPQETSP
CCCCCCCCCCCCCCC		48.6422167270
414PhosphorylationLDSQPQETSPELPRR
CCCCCCCCCCCCCHH		44.3129255136
415PhosphorylationDSQPQETSPELPRRR
CCCCCCCCCCCCHHH		18.6719664994
430PhosphorylationVRHQGDLSSGYLDDT
HCCCCCCCCCCCCCC		26.8522496350
431PhosphorylationRHQGDLSSGYLDDTK
CCCCCCCCCCCCCCC		38.4625159151
433PhosphorylationQGDLSSGYLDDTKQE
CCCCCCCCCCCCCCC		14.6525159151
437PhosphorylationSSGYLDDTKQETANG
CCCCCCCCCCCCCCC		34.0026074081
462PhosphorylationINNMTATYNQLSRST
CCCCEEHHHHHHCCC		9.8427642862
468PhosphorylationTYNQLSRSTSGPRPG
HHHHHHCCCCCCCCC		24.4525159151
469PhosphorylationYNQLSRSTSGPRPGC
HHHHHCCCCCCCCCC		36.2725159151
470PhosphorylationNQLSRSTSGPRPGCQ
HHHHCCCCCCCCCCC		48.3123401153
479PhosphorylationPRPGCQPSSPCVPKL
CCCCCCCCCCCCCCC		22.4925159151
480PhosphorylationRPGCQPSSPCVPKLS
CCCCCCCCCCCCCCC		29.0625159151
485UbiquitinationPSSPCVPKLSNSDSQ
CCCCCCCCCCCCCCC		44.1221890473
485UbiquitinationPSSPCVPKLSNSDSQ
CCCCCCCCCCCCCCC		44.1221890473
487PhosphorylationSPCVPKLSNSDSQDI
CCCCCCCCCCCCCCC		40.1721815630
489PhosphorylationCVPKLSNSDSQDIQG
CCCCCCCCCCCCCCC		34.9525394399
491PhosphorylationPKLSNSDSQDIQGRN
CCCCCCCCCCCCCCC		29.5822617229
501PhosphorylationIQGRNRDSQNGAIAP
CCCCCCCCCCCCCCC		23.4720068231
512PhosphorylationAIAPGHVSVIRPPQN
CCCCCEEEEECCCCC		13.2220068231
521PhosphorylationIRPPQNLYPENIVPS
ECCCCCCCCCCCCCC		18.9520873877
528PhosphorylationYPENIVPSFSPGPSG
CCCCCCCCCCCCCCC		27.7129214152
530PhosphorylationENIVPSFSPGPSGRY
CCCCCCCCCCCCCCC		33.0318669648
534PhosphorylationPSFSPGPSGRYGASG
CCCCCCCCCCCCCCC		41.6420068231
537PhosphorylationSPGPSGRYGASGRSE
CCCCCCCCCCCCCCC		22.1426074081
540PhosphorylationPSGRYGASGRSEGGR
CCCCCCCCCCCCCCC		30.31-
543PhosphorylationRYGASGRSEGGRNSR
CCCCCCCCCCCCCCC		44.0822461510
549PhosphorylationRSEGGRNSRVTPAAA
CCCCCCCCCCCHHHH		27.1121712546
552PhosphorylationGGRNSRVTPAAANYR
CCCCCCCCHHHHHHH		13.1925159151
558PhosphorylationVTPAAANYRSRTAKA
CCHHHHHHHHCCCCC		12.7728985074
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 TRAD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRAD1_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 TRAD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NGLY1_HUMANNGLY1physical
25416956
NAA15_HUMANNAA15physical
28514442
ACD11_HUMANACAD11physical
28514442
ASPM_HUMANASPMphysical
28514442
BTBD1_HUMANBTBD1physical
28514442
BBS4_HUMANBBS4physical
27173435
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 TRAD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-327 AND SER-415, AND MASS SPECTROMETRY.
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-327 AND SER-415, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-323; SER-327 ANDSER-415, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-327 AND SER-415, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-415 ANDSER-470, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-415, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-323; SER-327; THR-414AND SER-415, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-415, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASSSPECTROMETRY.
"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-415, AND MASSSPECTROMETRY.

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