DDX10_HUMAN - dbPTM
DDX10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX10_HUMAN
UniProt AC Q13206
Protein Name Probable ATP-dependent RNA helicase DDX10
Gene Name DDX10
Organism Homo sapiens (Human).
Sequence Length 875
Subcellular Localization
Protein Description Putative ATP-dependent RNA helicase..
Protein Sequence MGKTANSPGSGARPDPVRSFNRWKKKHSHRQNKKKQLRKQLKKPEWQVERESISRLMQNYEKINVNEITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETVSFHATDLQMLVLDEADRILDMGFADTMNAVIENLPKKRQTLLFSATQTKSVKDLARLSLKNPEYVWVHEKAKYSTPATLEQNYIVCELQQKISVLYSFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLRPGVSILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEKAMVQQLLQKKVPVKEIKINPEKLIDVQKKLESILAQDQDLKERAQRCFVSYVRSVYLMKDKEVFDVSKLPIPEYALSLGLAVAPRVRFLQKMQKQPTKELVRSQADKVIEPRAPSLTNDEVEEFRAYFNEKMSILQKGGKRLEGTEHRQDNDTGNEEQEEEEDDEEEMEEKLAKAKGSQAPSLPNTSEAQKIKEVPTQFLDRDEEEEDADFLKVKRHNVFGLDLKDEKTLQKKEPSKSSIKKKMTKVAEAKKVMKRNFKVNKKITFTDEGELVQQWPQMQKSAIKDAEEDDDTGGINLHKAKERLQEEDKFDKEEYRKKIKAKHREKRLKEREARREANKRQAKAKDEEEAFLDWSDDDDDDDDGFDPSTLPDPDKYRSSEDSDSEDMENKISDTKKKQGMKKRSNSEVEDVGPTSHNRKKARWDTLEPLDTGLSLAEDEELVLHLLRSQS
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
4Phosphorylation----MGKTANSPGSG
----CCCCCCCCCCC		25.9130266825
7Phosphorylation-MGKTANSPGSGARP
-CCCCCCCCCCCCCC		28.3325159151
10PhosphorylationKTANSPGSGARPDPV
CCCCCCCCCCCCCCC		32.4430266825
19PhosphorylationARPDPVRSFNRWKKK
CCCCCCHHHHHHHHH		27.4028555341
34UbiquitinationHSHRQNKKKQLRKQL
HHHHHHHHHHHHHHH		53.9924816145
52PhosphorylationEWQVERESISRLMQN
HHHHHHHHHHHHHHH		31.8920873877
54PhosphorylationQVERESISRLMQNYE
HHHHHHHHHHHHHHH		28.7420873877
60PhosphorylationISRLMQNYEKINVNE
HHHHHHHHHHCCHHH		11.1628509920
62UbiquitinationRLMQNYEKINVNEIT
HHHHHHHHCCHHHHH		29.2621906983
69PhosphorylationKINVNEITRFSDFPL
HCCHHHHHCCCCCCC		21.3426074081
72PhosphorylationVNEITRFSDFPLSKK
HHHHHCCCCCCCCHH		34.7426074081
77PhosphorylationRFSDFPLSKKTLKGL
CCCCCCCCHHHHHHH		32.1326074081
78UbiquitinationFSDFPLSKKTLKGLQ
CCCCCCCHHHHHHHH		58.4229967540
79UbiquitinationSDFPLSKKTLKGLQE
CCCCCCHHHHHHHHH		56.57-
80PhosphorylationDFPLSKKTLKGLQEA
CCCCCHHHHHHHHHH		37.1226074081
82UbiquitinationPLSKKTLKGLQEAQY
CCCHHHHHHHHHHHH		63.9129967540
89PhosphorylationKGLQEAQYRLVTEIQ
HHHHHHHHHHHHHHH		16.9824719451
93PhosphorylationEAQYRLVTEIQKQTI
HHHHHHHHHHHHHHH		31.7824719451
97UbiquitinationRLVTEIQKQTIGLAL
HHHHHHHHHHHCEEE		55.88-
107UbiquitinationIGLALQGKDVLGAAK
HCEEECCCCEECEEE		31.53-
114UbiquitinationKDVLGAAKTGSGKTL
CCEECEEECCCCHHH		53.5429967540
114AcetylationKDVLGAAKTGSGKTL
CCEECEEECCCCHHH		53.5425953088
117PhosphorylationLGAAKTGSGKTLAFL
ECEEECCCCHHHHHH		42.2022817900
179UbiquitinationAGLIIGGKDLKHEAE
EEEEECCCCHHHHHH		55.4629967540
197PhosphorylationNINILVCTPGRLLQH
CCEEEEECCCHHHHH		22.6925159151
208PhosphorylationLLQHMDETVSFHATD
HHHHHCCCEEEECCC		19.72-
249PhosphorylationNLPKKRQTLLFSATQ
HCCHHCCEEEEEECC		29.4821406692
253PhosphorylationKRQTLLFSATQTKSV
HCCEEEEEECCCCCH		30.3121406692
255PhosphorylationQTLLFSATQTKSVKD
CEEEEEECCCCCHHH		35.2620860994
257PhosphorylationLLFSATQTKSVKDLA
EEEEECCCCCHHHHH		22.4121406692
261UbiquitinationATQTKSVKDLARLSL
ECCCCCHHHHHHHHC		54.8629967540
269AcetylationDLARLSLKNPEYVWV
HHHHHHCCCCCEEEE		68.0626051181
269UbiquitinationDLARLSLKNPEYVWV
HHHHHHCCCCCEEEE		68.06-
273PhosphorylationLSLKNPEYVWVHEKA
HHCCCCCEEEEECCC		10.81-
279UbiquitinationEYVWVHEKAKYSTPA
CEEEEECCCCCCCCC		34.9929967540
281AcetylationVWVHEKAKYSTPATL
EEEECCCCCCCCCCH		51.2926051181
292PhosphorylationPATLEQNYIVCELQQ
CCCHHCCEEEHHHHH		8.40-
302PhosphorylationCELQQKISVLYSFLR
HHHHHHHHHHHHHHH		17.0720068231
305PhosphorylationQQKISVLYSFLRSHL
HHHHHHHHHHHHHHH		8.6720068231
306PhosphorylationQKISVLYSFLRSHLK
HHHHHHHHHHHHHHC		17.4020068231
341O-linked_GlycosylationCRLRPGVSILALHGR
HHHCCCCEEEEECCH		20.1430379171
358PhosphorylationQMRRMEVYNEFVRKR
HHHHHHHHHHHHHHH		8.8220860994
410UbiquitinationAGRTARYKEDGEALL
CCCCEEECCCCCEEE		43.72-
434UbiquitinationVQQLLQKKVPVKEIK
HHHHHHCCCCHHHCC		38.52-
446UbiquitinationEIKINPEKLIDVQKK
HCCCCHHHHHHHHHH		52.5829967540
453AcetylationKLIDVQKKLESILAQ
HHHHHHHHHHHHHHC		40.1620167786
453UbiquitinationKLIDVQKKLESILAQ
HHHHHHHHHHHHHHC		40.1629967540
465UbiquitinationLAQDQDLKERAQRCF
HHCCCCHHHHHHHHH		54.14-
515UbiquitinationPRVRFLQKMQKQPTK
HHHHHHHHHHHCCCH		45.50-
518UbiquitinationRFLQKMQKQPTKELV
HHHHHHHHCCCHHHH		55.5424816145
522UbiquitinationKMQKQPTKELVRSQA
HHHHCCCHHHHHHHC		56.59-
531AcetylationLVRSQADKVIEPRAP
HHHHHCCCCCCCCCC		48.4025953088
539PhosphorylationVIEPRAPSLTNDEVE
CCCCCCCCCCHHHHH		47.0129255136
541PhosphorylationEPRAPSLTNDEVEEF
CCCCCCCCHHHHHHH		44.9830266825
555AcetylationFRAYFNEKMSILQKG
HHHHHHHHHHHHHHC		38.77-
569PhosphorylationGGKRLEGTEHRQDND
CCCCCCCCCCCCCCC		21.1723927012
577PhosphorylationEHRQDNDTGNEEQEE
CCCCCCCCCCHHHHH		48.4326503892
602PhosphorylationKLAKAKGSQAPSLPN
HHHHHCCCCCCCCCC		23.5922199227
606PhosphorylationAKGSQAPSLPNTSEA
HCCCCCCCCCCCHHH		60.5222199227
610PhosphorylationQAPSLPNTSEAQKIK
CCCCCCCCHHHHHHH		26.4622199227
610O-linked_GlycosylationQAPSLPNTSEAQKIK
CCCCCCCCHHHHHHH		26.4630379171
611O-linked_GlycosylationAPSLPNTSEAQKIKE
CCCCCCCHHHHHHHH		37.2630379171
611PhosphorylationAPSLPNTSEAQKIKE
CCCCCCCHHHHHHHH		37.2622199227
626MethylationVPTQFLDRDEEEEDA
CCCCCCCCCCHHCCC		56.22-
649SumoylationNVFGLDLKDEKTLQK
CCCCCCCCCHHHHCC		64.6028112733
649AcetylationNVFGLDLKDEKTLQK
CCCCCCCCCHHHHCC		64.6026051181
652UbiquitinationGLDLKDEKTLQKKEP
CCCCCCHHHHCCCCC		65.7522817900
656UbiquitinationKDEKTLQKKEPSKSS
CCHHHHCCCCCCHHH		63.3222817900
657UbiquitinationDEKTLQKKEPSKSSI
CHHHHCCCCCCHHHH		62.9922817900
660PhosphorylationTLQKKEPSKSSIKKK
HHCCCCCCHHHHHHH		46.3821406692
661UbiquitinationLQKKEPSKSSIKKKM
HCCCCCCHHHHHHHH		59.9622817900
662PhosphorylationQKKEPSKSSIKKKMT
CCCCCCHHHHHHHHH		41.4525159151
663PhosphorylationKKEPSKSSIKKKMTK
CCCCCHHHHHHHHHH		42.0125159151
666AcetylationPSKSSIKKKMTKVAE
CCHHHHHHHHHHHHH		46.2230588043
670AcetylationSIKKKMTKVAEAKKV
HHHHHHHHHHHHHHH		35.6330588049
709AcetylationQMQKSAIKDAEEDDD
HHHHHHHCCCCCCCC		51.0726051181
717PhosphorylationDAEEDDDTGGINLHK
CCCCCCCCCCCCHHH		44.2825159151
734UbiquitinationERLQEEDKFDKEEYR
HHHHHHCCCCHHHHH		59.7624816145
780PhosphorylationEEAFLDWSDDDDDDD
HHHHCCCCCCCCCCC		30.7221082442
793PhosphorylationDDDGFDPSTLPDPDK
CCCCCCHHHCCCHHH		44.4122496350
794PhosphorylationDDGFDPSTLPDPDKY
CCCCCHHHCCCHHHC		47.9321406692
801PhosphorylationTLPDPDKYRSSEDSD
HCCCHHHCCCCCCCC		24.0920363803
803PhosphorylationPDPDKYRSSEDSDSE
CCHHHCCCCCCCCCH		34.6820873877
804PhosphorylationDPDKYRSSEDSDSED
CHHHCCCCCCCCCHH		36.1020363803
807PhosphorylationKYRSSEDSDSEDMEN
HCCCCCCCCCHHHHH		38.7020363803
809PhosphorylationRSSEDSDSEDMENKI
CCCCCCCCHHHHHHH		39.1720363803
829PhosphorylationKQGMKKRSNSEVEDV
HHCCCCCCCCCCCCC		54.2925463755
831PhosphorylationGMKKRSNSEVEDVGP
CCCCCCCCCCCCCCC		44.2429255136
839PhosphorylationEVEDVGPTSHNRKKA
CCCCCCCCCCCCCCC		36.3725159151
840PhosphorylationVEDVGPTSHNRKKAR
CCCCCCCCCCCCCCC		23.1525159151
873PhosphorylationLVLHLLRSQS-----
HHHHHHHHCC-----		34.4426074081
875PhosphorylationLHLLRSQS-------
HHHHHHCC-------		43.3626074081
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 DDX10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX10_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 DDX10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DDX54_HUMANDDX54physical
26344197
PWP1_HUMANPWP1physical
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 DDX10_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-539, AND MASSSPECTROMETRY.
"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-539 AND THR-577, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-7, 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-7 AND SER-539, 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-780, AND MASSSPECTROMETRY.
"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 THR-569, AND MASSSPECTROMETRY.

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