DDX20_HUMAN - dbPTM
DDX20_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX20_HUMAN
UniProt AC Q9UHI6
Protein Name Probable ATP-dependent RNA helicase DDX20
Gene Name DDX20
Organism Homo sapiens (Human).
Sequence Length 824
Subcellular Localization Cytoplasm. Nucleus, gem. Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems).
Protein Description The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)..
Protein Sequence MAAAFEASGALAAVATAMPAEHVAVQVPAPEPTPGPVRILRTAQDLSSPRTRTGDVLLAEPADFESLLLSRPVLEGLRAAGFERPSPVQLKAIPLGRCGLDLIVQAKSGTGKTCVFSTIALDSLVLENLSTQILILAPTREIAVQIHSVITAIGIKMEGLECHVFIGGTPLSQDKTRLKKCHIAVGSPGRIKQLIELDYLNPGSIRLFILDEADKLLEEGSFQEQINWIYSSLPASKQMLAVSATYPEFLANALTKYMRDPTFVRLNSSDPSLIGLKQYYKVVNSYPLAHKVFEEKTQHLQELFSRIPFNQALVFSNLHSRAQHLADILSSKGFPAECISGNMNQNQRLDAMAKLKHFHCRVLISTDLTSRGIDAEKVNLVVNLDVPLDWETYMHRIGRAGRFGTLGLTVTYCCRGEEENMMMRIAQKCNINLLPLPDPIPSGLMEECVDWDVEVKAAVHTYGIASVPNQPLKKQIQKIERTLQIQKAHGDHMASSRNNSVSGLSVKSKNNTKQKLPVKSHSECGIIEKATSPKELGCDRQSEEQMKNSVQTPVENSTNSQHQVKEALPVSLPQIPCLSSFKIHQPYTLTFAELVEDYEHYIKEGLEKPVEIIRHYTGPGDQTVNPQNGFVRNKVIEQRVPVLASSSQSGDSESDSDSYSSRTSSQSKGNKSYLEGSSDNQLKDSESTPVDDRISLEQPPNGSDTPNPEKYQESPGIQMKTRLKEGASQRAKQSRRNLPRRSSFRLQTEAQEDDWYDCHREIRLSFSDTYQDYEEYWRAYYRAWQEYYAAASHSYYWNAQRHPSWMAAYHMNTIYLQEMMHSNQ
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
33PhosphorylationQVPAPEPTPGPVRIL
ECCCCCCCCCCEEEE		38.9324173317
42PhosphorylationGPVRILRTAQDLSSP
CCEEEEEEHHHCCCC		25.8127251275
47PhosphorylationLRTAQDLSSPRTRTG
EEEHHHCCCCCCCCC		46.7329255136
48PhosphorylationRTAQDLSSPRTRTGD
EEHHHCCCCCCCCCC		26.2129255136
86PhosphorylationAAGFERPSPVQLKAI
HCCCCCCCCCEEEEE		43.8820068231
91UbiquitinationRPSPVQLKAIPLGRC
CCCCCEEEEECCCCC		27.4621890473
91AcetylationRPSPVQLKAIPLGRC
CCCCCEEEEECCCCC		27.4626051181
91UbiquitinationRPSPVQLKAIPLGRC
CCCCCEEEEECCCCC		27.4621890473
107UbiquitinationLDLIVQAKSGTGKTC
CEEEEEECCCCCCCC		32.12-
175AcetylationGTPLSQDKTRLKKCH
CEECCCCCHHHCCCE		28.1026051181
175UbiquitinationGTPLSQDKTRLKKCH
CEECCCCCHHHCCCE		28.10-
180UbiquitinationQDKTRLKKCHIAVGS
CCCHHHCCCEEECCC		35.32-
187PhosphorylationKCHIAVGSPGRIKQL
CCEEECCCCCHHHHH		19.9930266825
192UbiquitinationVGSPGRIKQLIELDY
CCCCCHHHHHEECCC		37.38-
199PhosphorylationKQLIELDYLNPGSIR
HHHEECCCCCCCCEE		22.47-
245PhosphorylationQMLAVSATYPEFLAN
HHHHHHCCCHHHHHH		31.9120860994
255PhosphorylationEFLANALTKYMRDPT
HHHHHHHHHHHCCCC		20.0920860994
262PhosphorylationTKYMRDPTFVRLNSS
HHHHCCCCEEECCCC		38.7723403867
268PhosphorylationPTFVRLNSSDPSLIG
CCEEECCCCCHHHHC		40.4830266825
269PhosphorylationTFVRLNSSDPSLIGL
CEEECCCCCHHHHCH		53.0930266825
272PhosphorylationRLNSSDPSLIGLKQY
ECCCCCHHHHCHHHH		37.2930266825
277UbiquitinationDPSLIGLKQYYKVVN
CHHHHCHHHHHHHHH		30.92-
279PhosphorylationSLIGLKQYYKVVNSY
HHHCHHHHHHHHHHH		12.0323312004
280PhosphorylationLIGLKQYYKVVNSYP
HHCHHHHHHHHHHHH		8.5323312004
281UbiquitinationIGLKQYYKVVNSYPL
HCHHHHHHHHHHHHH		34.47-
291UbiquitinationNSYPLAHKVFEEKTQ
HHHHHHHHHHHHHHH		42.91-
2962-HydroxyisobutyrylationAHKVFEEKTQHLQEL
HHHHHHHHHHHHHHH		46.41-
296AcetylationAHKVFEEKTQHLQEL
HHHHHHHHHHHHHHH		46.4126051181
296UbiquitinationAHKVFEEKTQHLQEL
HHHHHHHHHHHHHHH		46.41-
320PhosphorylationLVFSNLHSRAQHLAD
HHHCCCHHHHHHHHH		32.2629523821
332AcetylationLADILSSKGFPAECI
HHHHHHCCCCCHHHH		62.2826051181
332UbiquitinationLADILSSKGFPAECI
HHHHHHCCCCCHHHH		62.28-
354AcetylationQRLDAMAKLKHFHCR
HHHHHHHHHCHHCEE		45.0125953088
354UbiquitinationQRLDAMAKLKHFHCR
HHHHHHHHHCHHCEE		45.01-
365PhosphorylationFHCRVLISTDLTSRG
HCEEEEECCCCCCCC		16.2320068231
366PhosphorylationHCRVLISTDLTSRGI
CEEEEECCCCCCCCC		28.2128555341
392PhosphorylationDVPLDWETYMHRIGR
CCCCCHHHHHHHHHC		23.1428450419
393PhosphorylationVPLDWETYMHRIGRA
CCCCHHHHHHHHHCC		4.5728450419
442PhosphorylationPLPDPIPSGLMEECV
CCCCCCCCCHHHHHC		45.32-
461PhosphorylationEVKAAVHTYGIASVP
HHHHHHHHCCCCCCC		19.4928152594
462PhosphorylationVKAAVHTYGIASVPN
HHHHHHHCCCCCCCC		7.5228152594
466PhosphorylationVHTYGIASVPNQPLK
HHHCCCCCCCCCCHH		35.8728442448
473UbiquitinationSVPNQPLKKQIQKIE
CCCCCCHHHHHHHHH		49.68-
474AcetylationVPNQPLKKQIQKIER
CCCCCHHHHHHHHHH		61.3925953088
474UbiquitinationVPNQPLKKQIQKIER
CCCCCHHHHHHHHHH		61.39-
478UbiquitinationPLKKQIQKIERTLQI
CHHHHHHHHHHHHHH		48.43-
482PhosphorylationQIQKIERTLQIQKAH
HHHHHHHHHHHHHHH		15.3823403867
487MethylationERTLQIQKAHGDHMA
HHHHHHHHHHHHHHC		43.94-
487UbiquitinationERTLQIQKAHGDHMA
HHHHHHHHHHHHHHC		43.94-
495PhosphorylationAHGDHMASSRNNSVS
HHHHHHCCCCCCCCC		23.4322496350
496PhosphorylationHGDHMASSRNNSVSG
HHHHHCCCCCCCCCC		29.5022496350
500PhosphorylationMASSRNNSVSGLSVK
HCCCCCCCCCCEEEE		22.6222167270
502PhosphorylationSSRNNSVSGLSVKSK
CCCCCCCCCEEEECC		33.5622167270
505PhosphorylationNNSVSGLSVKSKNNT
CCCCCCEEEECCCCC		30.9023401153
507AcetylationSVSGLSVKSKNNTKQ
CCCCEEEECCCCCCC		52.9525953088
507UbiquitinationSVSGLSVKSKNNTKQ
CCCCEEEECCCCCCC		52.95-
519UbiquitinationTKQKLPVKSHSECGI
CCCCCCCCCCCCCCC		40.28-
520PhosphorylationKQKLPVKSHSECGII
CCCCCCCCCCCCCCE		32.2628450419
522PhosphorylationKLPVKSHSECGIIEK
CCCCCCCCCCCCEEC		41.4925159151
529AcetylationSECGIIEKATSPKEL
CCCCCEECCCCHHHH		46.7026051181
529UbiquitinationSECGIIEKATSPKEL
CCCCCEECCCCHHHH		46.70-
531PhosphorylationCGIIEKATSPKELGC
CCCEECCCCHHHHCC		57.5422617229
532PhosphorylationGIIEKATSPKELGCD
CCEECCCCHHHHCCC		38.5423401153
534UbiquitinationIEKATSPKELGCDRQ
EECCCCHHHHCCCCC		66.40-
542PhosphorylationELGCDRQSEEQMKNS
HHCCCCCCHHHHHHH		43.9525159151
547AcetylationRQSEEQMKNSVQTPV
CCCHHHHHHHCCCCC		45.8526051181
549PhosphorylationSEEQMKNSVQTPVEN
CHHHHHHHCCCCCCC		15.3027732954
552PhosphorylationQMKNSVQTPVENSTN
HHHHHCCCCCCCCCC		27.4425159151
557PhosphorylationVQTPVENSTNSQHQV
CCCCCCCCCCCHHHH		18.5625159151
558PhosphorylationQTPVENSTNSQHQVK
CCCCCCCCCCHHHHH		50.9325159151
560PhosphorylationPVENSTNSQHQVKEA
CCCCCCCCHHHHHHH		29.1825159151
565UbiquitinationTNSQHQVKEALPVSL
CCCHHHHHHHCCCCC		30.60-
571PhosphorylationVKEALPVSLPQIPCL
HHHHCCCCCCCCCCC		32.1827080861
579PhosphorylationLPQIPCLSSFKIHQP
CCCCCCCCCCCCCCC		40.2127080861
580PhosphorylationPQIPCLSSFKIHQPY
CCCCCCCCCCCCCCE		20.0127080861
608UbiquitinationYIKEGLEKPVEIIRH
HHHHCCCCCEEEEEC		60.45-
616PhosphorylationPVEIIRHYTGPGDQT
CEEEEECCCCCCCCC		11.9825159151
617PhosphorylationVEIIRHYTGPGDQTV
EEEEECCCCCCCCCC		30.6728555341
634UbiquitinationQNGFVRNKVIEQRVP
CCCCCCCCHHHCCCC		33.74-
645PhosphorylationQRVPVLASSSQSGDS
CCCCEEEECCCCCCC		26.7630177828
646PhosphorylationRVPVLASSSQSGDSE
CCCEEEECCCCCCCC		27.1330177828
647PhosphorylationVPVLASSSQSGDSES
CCEEEECCCCCCCCC		26.3530177828
649PhosphorylationVLASSSQSGDSESDS
EEEECCCCCCCCCCC		46.6518669648
652PhosphorylationSSSQSGDSESDSDSY
ECCCCCCCCCCCCCC		42.3918669648
654PhosphorylationSQSGDSESDSDSYSS
CCCCCCCCCCCCCCC		46.4925159151
656PhosphorylationSGDSESDSDSYSSRT
CCCCCCCCCCCCCCC		37.4218669648
658PhosphorylationDSESDSDSYSSRTSS
CCCCCCCCCCCCCCC		30.7630177828
659PhosphorylationSESDSDSYSSRTSSQ
CCCCCCCCCCCCCCC		18.6930177828
660PhosphorylationESDSDSYSSRTSSQS
CCCCCCCCCCCCCCC		19.8030177828
661PhosphorylationSDSDSYSSRTSSQSK
CCCCCCCCCCCCCCC		31.2030177828
667PhosphorylationSSRTSSQSKGNKSYL
CCCCCCCCCCCCHHC		44.4728787133
671AcetylationSSQSKGNKSYLEGSS
CCCCCCCCHHCCCCC		49.5026051181
671UbiquitinationSSQSKGNKSYLEGSS
CCCCCCCCHHCCCCC		49.50-
672PhosphorylationSQSKGNKSYLEGSSD
CCCCCCCHHCCCCCC		38.6623927012
673PhosphorylationQSKGNKSYLEGSSDN
CCCCCCHHCCCCCCC		15.4723927012
677PhosphorylationNKSYLEGSSDNQLKD
CCHHCCCCCCCCCCC		25.7429255136
678PhosphorylationKSYLEGSSDNQLKDS
CHHCCCCCCCCCCCC		51.9819664994
683AcetylationGSSDNQLKDSESTPV
CCCCCCCCCCCCCCC		49.8226051181
683UbiquitinationGSSDNQLKDSESTPV
CCCCCCCCCCCCCCC		49.82-
685PhosphorylationSDNQLKDSESTPVDD
CCCCCCCCCCCCCCC		31.6823927012
687PhosphorylationNQLKDSESTPVDDRI
CCCCCCCCCCCCCCC		41.8023927012
688PhosphorylationQLKDSESTPVDDRIS
CCCCCCCCCCCCCCC		24.2325159151
693MethylationESTPVDDRISLEQPP
CCCCCCCCCCCCCCC		18.87-
695PhosphorylationTPVDDRISLEQPPNG
CCCCCCCCCCCCCCC		27.0922167270
703PhosphorylationLEQPPNGSDTPNPEK
CCCCCCCCCCCCHHH		44.9719664994
705PhosphorylationQPPNGSDTPNPEKYQ
CCCCCCCCCCHHHHC		27.0229255136
710UbiquitinationSDTPNPEKYQESPGI
CCCCCHHHHCCCCCC		54.19-
711PhosphorylationDTPNPEKYQESPGIQ
CCCCHHHHCCCCCCC		18.8222167270
714PhosphorylationNPEKYQESPGIQMKT
CHHHHCCCCCCCCHH		16.9519664994
720MethylationESPGIQMKTRLKEGA
CCCCCCCHHHHHHHH		17.70-
720UbiquitinationESPGIQMKTRLKEGA
CCCCCCCHHHHHHHH		17.70-
728PhosphorylationTRLKEGASQRAKQSR
HHHHHHHHHHHHHHH		30.9324732914
742PhosphorylationRRNLPRRSSFRLQTE
HHCCCCCHHCCCCCC		34.8030624053
743PhosphorylationRNLPRRSSFRLQTEA
HCCCCCHHCCCCCCC		16.7527422710
748PhosphorylationRSSFRLQTEAQEDDW
CHHCCCCCCCCCCCH		37.5729978859
756PhosphorylationEAQEDDWYDCHREIR
CCCCCCHHHHCHHHC		18.7128796482
765PhosphorylationCHREIRLSFSDTYQD
HCHHHCCCCCCCCCC		16.9223663014
767PhosphorylationREIRLSFSDTYQDYE
HHHCCCCCCCCCCHH		26.1823663014
769PhosphorylationIRLSFSDTYQDYEEY
HCCCCCCCCCCHHHH		23.1427080861
770PhosphorylationRLSFSDTYQDYEEYW
CCCCCCCCCCHHHHH		12.3627642862
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 DDX20_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX20_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 DDX20_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GEMI5_HUMANGEMIN5physical
11714716
GEMI2_HUMANGEMIN2physical
11914277
GEMI4_HUMANGEMIN4physical
11914277
GEMI5_HUMANGEMIN5physical
11914277
AGO2_HUMANAGO2physical
11914277
SMN_HUMANSMN1physical
11914277
LSM2_HUMANLSM2physical
10601333
RUXG_HUMANSNRPGphysical
10601333
RUXF_HUMANSNRPFphysical
10601333
SMD3_HUMANSNRPD3physical
10601333
SMD2_HUMANSNRPD2physical
10601333
SMN_HUMANSMN1physical
10601333
RSMB_HUMANSNRPBphysical
10601333
RUXE_HUMANSNRPEphysical
10601333
GEMI2_HUMANGEMIN2physical
10601333
SMD1_HUMANSNRPD1physical
10601333
A4_HUMANAPPphysical
21832049
SMN_HUMANSMN1physical
22939629
HDA11_HUMANHDAC11physical
23752268
SMN_HUMANSMN1physical
23752268
DDX20_HUMANDDX20physical
23752268
GEMI4_HUMANGEMIN4physical
23752268
DICER_HUMANDICER1physical
23752268
GEMI8_HUMANGEMIN8physical
28514442
GEMI2_HUMANGEMIN2physical
28514442
USO1_HUMANUSO1physical
28514442
GEMI5_HUMANGEMIN5physical
28514442
GEMI6_HUMANGEMIN6physical
28514442
GEMI4_HUMANGEMIN4physical
28514442
RU17_HUMANSNRNP70physical
28514442
LSM11_HUMANLSM11physical
28514442
STRAP_HUMANSTRAPphysical
28514442
PHAX_HUMANPHAXphysical
28514442
GEMI7_HUMANGEMIN7physical
28514442
G3PT_HUMANGAPDHSphysical
28514442
CPSF7_HUMANCPSF7physical
28514442
EAF1_HUMANEAF1physical
27173435
NAF1_HUMANNAF1physical
27173435
ATRX_HUMANATRXphysical
27173435
DPOD1_HUMANPOLD1physical
27173435
RBM14_HUMANRBM14physical
27173435
MFAP1_HUMANMFAP1physical
27173435
MCM3_HUMANMCM3physical
27173435
NUFP1_HUMANNUFIP1physical
26275778
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 DDX20_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-677; SER-678 ANDSER-703, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678; SER-703;THR-705 AND SER-714, 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-48; SER-500; SER-532;THR-552; SER-649; SER-652; SER-654; SER-656; SER-672; SER-677;SER-678; SER-703; THR-705 AND SER-714, 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-48; SER-187; THR-552;SER-677; SER-678; THR-705 AND SER-714, AND MASS 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 SER-678, AND MASSSPECTROMETRY.
"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-714, 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-500, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-705 AND SER-714, ANDMASS SPECTROMETRY.

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