DDX54_HUMAN - dbPTM
DDX54_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX54_HUMAN
UniProt AC Q8TDD1
Protein Name ATP-dependent RNA helicase DDX54
Gene Name DDX54
Organism Homo sapiens (Human).
Sequence Length 881
Subcellular Localization Nucleus, nucleolus .
Protein Description Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors..
Protein Sequence MAADKGPAAGPRSRAAMAQWRKKKGLRKRRGAASQARGSDSEDGEFEIQAEDDARARKLGPGRPLPTFPTSECTSDVEPDTREMVRAQNKKKKKSGGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGARALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLHNVVRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSLTLARPLKEPSGVAGVDGMLGRVPQSVVDEEDSGLQSTLEASLELRGLARVADNAQQQYVRSRPAPSPESIKRAKEMDLVGLGLHPLFSSRFEEEELQRLRLVDSIKNYRSRATIFEINASSRDLCSQVMRAKRQKDRKAIARFQQGQQGRQEQQEGPVGPAPSRPALQEKQPEKEEEEEAGESVEDIFSEVVGRKRQRSGPNRGAKRRREEARQRDQEFYIPYRPKDFDSERGLSISGEGGAFEQQAAGAVLDLMGDEAQNLTRGRQQLKWDRKKKRFVGQSGQEDKKKIKTESGRYISSSYKRDLYQKWKQKQKIDDRDSDEEGASDRRGPERRGGKRDRGQGASRPHAPGTPAGRVRPELKTKQQILKQRRRAQKLHFLQRGGLKQLSARNRRRVQELQQGAFGRGARSKKGKMRKRM
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------MAADKGPAA
------CCCCCCCCC		25.11-
5Acetylation---MAADKGPAAGPR
---CCCCCCCCCCHH		63.1725953088
5Ubiquitination---MAADKGPAAGPR
---CCCCCCCCCCHH		63.1729967540
34PhosphorylationRKRRGAASQARGSDS
HHHCCCHHHCCCCCC		24.6820164059
34 (in isoform 2)Phosphorylation-24.6824719451
39PhosphorylationAASQARGSDSEDGEF
CHHHCCCCCCCCCCE		32.2029255136
39 (in isoform 2)Phosphorylation-32.2024719451
41PhosphorylationSQARGSDSEDGEFEI
HHCCCCCCCCCCEEE		39.0129255136
41 (in isoform 2)Phosphorylation-39.0124719451
67PhosphorylationGPGRPLPTFPTSECT
CCCCCCCCCCCCCCC		50.3523927012
70PhosphorylationRPLPTFPTSECTSDV
CCCCCCCCCCCCCCC		32.7329209046
71PhosphorylationPLPTFPTSECTSDVE
CCCCCCCCCCCCCCC		30.8020201521
74PhosphorylationTFPTSECTSDVEPDT
CCCCCCCCCCCCCCH		24.7429255136
74 (in isoform 2)Phosphorylation-24.7427251275
75PhosphorylationFPTSECTSDVEPDTR
CCCCCCCCCCCCCHH		51.8519664994
75 (in isoform 2)Phosphorylation-51.8524719451
81PhosphorylationTSDVEPDTREMVRAQ
CCCCCCCHHHHHHHH		38.9623927012
95PhosphorylationQNKKKKKSGGFQSMG
HHHHCCCCCCCCCCC		53.6923403867
100PhosphorylationKKSGGFQSMGLSYPV
CCCCCCCCCCCCHHH		16.7422199227
104PhosphorylationGFQSMGLSYPVFKGI
CCCCCCCCHHHHHHH		22.9723403867
105PhosphorylationFQSMGLSYPVFKGIM
CCCCCCCHHHHHHHH		14.4122199227
109AcetylationGLSYPVFKGIMKKGY
CCCHHHHHHHHHCCC		48.0026051181
116PhosphorylationKGIMKKGYKVPTPIQ
HHHHHCCCCCCCCCC		20.07-
120PhosphorylationKKGYKVPTPIQRKTI
HCCCCCCCCCCCCCC		35.6920068231
134AcetylationIPVILDGKDVVAMAR
CCEEECCCCEEEEEE		47.2026051181
142PhosphorylationDVVAMARTGSGKTAC
CEEEEEECCCCHHHH		26.59-
146AcetylationMARTGSGKTACFLLP
EEECCCCHHHHHHHH		34.3526051181
147PhosphorylationARTGSGKTACFLLPM
EECCCCHHHHHHHHH		31.98-
149GlutathionylationTGSGKTACFLLPMFE
CCCCHHHHHHHHHHH		2.7522555962
159UbiquitinationLPMFERLKTHSAQTG
HHHHHHHHHCCCCCC		50.8729967540
162PhosphorylationFERLKTHSAQTGARA
HHHHHHCCCCCCCCH		27.57-
173PhosphorylationGARALILSPTRELAL
CCCHHHCCCCHHHHH		19.7527067055
182PhosphorylationTRELALQTLKFTKEL
CHHHHHHHHHHHHHH		32.5320068231
184AcetylationELALQTLKFTKELGK
HHHHHHHHHHHHHCC		55.1425953088
184MalonylationELALQTLKFTKELGK
HHHHHHHHHHHHHCC		55.1426320211
184 (in isoform 2)Ubiquitination-55.14-
186PhosphorylationALQTLKFTKELGKFT
HHHHHHHHHHHCCCC		23.25-
187AcetylationLQTLKFTKELGKFTG
HHHHHHHHHHCCCCC		54.8226051181
191AcetylationKFTKELGKFTGLKTA
HHHHHHCCCCCCCEE		52.9926051181
196AcetylationLGKFTGLKTALILGG
HCCCCCCCEEEEECC		32.8526051181
197PhosphorylationGKFTGLKTALILGGD
CCCCCCCEEEEECCC		31.5724114839
223PhosphorylationNPDIIIATPGRLVHV
CCCEEEECCCCCCCH		18.8327050516
235PhosphorylationVHVAVEMSLKLQSVE
CCHHHHHHHHCCCCE		14.6228509920
243PhosphorylationLKLQSVEYVVFDEAD
HHCCCCEEEEEECHH		10.3528509920
306AcetylationIRLDVDTKLNEQLKT
EEEECCCHHHHHHHH		44.8726051181
312MethylationTKLNEQLKTSFFLVR
CHHHHHHHHEEEEEC		41.64-
378UbiquitinationALDPTARKINLAKFT
HCCCHHHHCHHHHHH		33.2223000965
383AcetylationARKINLAKFTLGKCS
HHHCHHHHHHHCCCC		41.8926051181
383UbiquitinationARKINLAKFTLGKCS
HHHCHHHHHHHCCCC		41.8923000965
383 (in isoform 2)Ubiquitination-41.89-
388AcetylationLAKFTLGKCSTLIVT
HHHHHHCCCCEEEHH		28.2926051181
388UbiquitinationLAKFTLGKCSTLIVT
HHHHHHCCCCEEEHH		28.2923000965
418UbiquitinationINYSFPAKGKLFLHR
CCCCCCCCCCEEHHH		57.74-
418 (in isoform 2)Ubiquitination-57.74-
420AcetylationYSFPAKGKLFLHRVG
CCCCCCCCEEHHHHH		35.0526051181
420UbiquitinationYSFPAKGKLFLHRVG
CCCCCCCCEEHHHHH		35.05-
420 (in isoform 2)Ubiquitination-35.05-
460PhosphorylationLHLFLGRSLTLARPL
HHHHHCCCCHHCCCC		24.7321406692
462PhosphorylationLFLGRSLTLARPLKE
HHHCCCCHHCCCCCC		21.4421406692
468UbiquitinationLTLARPLKEPSGVAG
CHHCCCCCCCCCCCC		70.9724816145
468 (in isoform 2)Ubiquitination-70.97-
471PhosphorylationARPLKEPSGVAGVDG
CCCCCCCCCCCCCCC		47.1720068231
497PhosphorylationEEDSGLQSTLEASLE
CCCCCHHHHHHHHHH		39.75-
502PhosphorylationLQSTLEASLELRGLA
HHHHHHHHHHHHHHH		17.0124719451
519PhosphorylationADNAQQQYVRSRPAP
HHHHHHHHHHCCCCC		8.0928152594
522PhosphorylationAQQQYVRSRPAPSPE
HHHHHHHCCCCCCHH		32.3523186163
527PhosphorylationVRSRPAPSPESIKRA
HHCCCCCCHHHHHHH		43.3225159151
530PhosphorylationRPAPSPESIKRAKEM
CCCCCHHHHHHHHHC		36.4730576142
532UbiquitinationAPSPESIKRAKEMDL
CCCHHHHHHHHHCCC		56.4324816145
535AcetylationPESIKRAKEMDLVGL
HHHHHHHHHCCCCCC		58.5726051181
535UbiquitinationPESIKRAKEMDLVGL
HHHHHHHHHCCCCCC		58.57-
535 (in isoform 2)Ubiquitination-58.57-
565PhosphorylationQRLRLVDSIKNYRSR
HHHHHHHHHHCHHHC		28.1626434776
567AcetylationLRLVDSIKNYRSRAT
HHHHHHHHCHHHCCE		52.4526051181
567UbiquitinationLRLVDSIKNYRSRAT
HHHHHHHHCHHHCCE		52.45-
567 (in isoform 2)Ubiquitination-52.45-
571PhosphorylationDSIKNYRSRATIFEI
HHHHCHHHCCEEEEE		18.8629457462
581PhosphorylationTIFEINASSRDLCSQ
EEEEECCCHHHHHHH		22.7828555341
624PhosphorylationGPVGPAPSRPALQEK
CCCCCCCCCHHHHCC		53.6630576142
644PhosphorylationEEEEAGESVEDIFSE
HHHHHCCCHHHHHHH		29.8630266825
644 (in isoform 2)Phosphorylation-29.8624719451
650PhosphorylationESVEDIFSEVVGRKR
CCHHHHHHHHHCCHH		29.8028176443
660PhosphorylationVGRKRQRSGPNRGAK
HCCHHHCCCCCHHHH		50.71-
681PhosphorylationRQRDQEFYIPYRPKD
HHHCCCCCCCCCCCC		10.5529978859
684PhosphorylationDQEFYIPYRPKDFDS
CCCCCCCCCCCCCCC		29.9529978859
687AcetylationFYIPYRPKDFDSERG
CCCCCCCCCCCCCCC		63.1326051181
696PhosphorylationFDSERGLSISGEGGA
CCCCCCCCCCCCCCH		19.9620068231
696 (in isoform 2)Phosphorylation-19.9627251275
698PhosphorylationSERGLSISGEGGAFE
CCCCCCCCCCCCHHH		27.6720068231
743PhosphorylationKKRFVGQSGQEDKKK
HCCCCCCCCCCCHHH		36.1925159151
752UbiquitinationQEDKKKIKTESGRYI
CCCHHHCCCCCCCCC		55.9324816145
753PhosphorylationEDKKKIKTESGRYIS
CCHHHCCCCCCCCCC		38.57-
755PhosphorylationKKKIKTESGRYISSS
HHHCCCCCCCCCCCH		33.53-
762PhosphorylationSGRYISSSYKRDLYQ
CCCCCCCHHHHHHHH		28.0828555341
764UbiquitinationRYISSSYKRDLYQKW
CCCCCHHHHHHHHHH		41.19-
782PhosphorylationQKIDDRDSDEEGASD
CCCCCCCCCCCCCCC		48.0629255136
782 (in isoform 2)Phosphorylation-48.0624719451
788PhosphorylationDSDEEGASDRRGPER
CCCCCCCCCCCCCCC		42.3722167270
802DimethylationRRGGKRDRGQGASRP
CCCCCCCCCCCCCCC		43.28-
807PhosphorylationRDRGQGASRPHAPGT
CCCCCCCCCCCCCCC		53.8430257219
808 (in isoform 2)Phosphorylation-26.8723927012
814PhosphorylationSRPHAPGTPAGRVRP
CCCCCCCCCCCCCCH		14.6530576142
815PhosphorylationRPHAPGTPAGRVRPE
CCCCCCCCCCCCCHH		38.3432645325
815 (in isoform 2)Phosphorylation-38.3423927012
820DimethylationGTPAGRVRPELKTKQ
CCCCCCCCHHHHHHH		20.02-
844MethylationQKLHFLQRGGLKQLS
HHHHHHHHCCHHHHH		43.21-
851PhosphorylationRGGLKQLSARNRRRV
HCCHHHHHHHHHHHH		23.7626434776
868MethylationLQQGAFGRGARSKKG
HHHCCCCCCCCCCCC		29.19-
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 DDX54_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX54_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 DDX54_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR1_HUMANESR1physical
12466272
ESR2_HUMANESR2physical
12466272
GCR_HUMANNR3C1physical
12466272
PRGR_HUMANPGRphysical
12466272
A4_HUMANAPPphysical
21832049
SEM4A_HUMANSEMA4Aphysical
21988832
RPB7_HUMANPOLR2Gphysical
21988832
TMED9_HUMANTMED9physical
21988832
LA_HUMANSSBphysical
26344197
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 DDX54_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 THR-74 AND SER-75, 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-34; SER-39; SER-41 ANDSER-782, 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 THR-74 AND SER-75, 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-34; SER-39; SER-41;SER-75; SER-644; SER-782 AND SER-788, 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-782, 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-39; SER-41 AND SER-782,AND MASS SPECTROMETRY.

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