DDX17_HUMAN - dbPTM
DDX17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX17_HUMAN
UniProt AC Q92841
Protein Name Probable ATP-dependent RNA helicase DDX17
Gene Name DDX17
Organism Homo sapiens (Human).
Sequence Length 729
Subcellular Localization Nucleus . Nucleus, nucleolus . Cytoplasm, cytosol . In the course of bunyavirus infection, relocalizes from the nucleus to the cytosol where it binds viral RNA to antagonize replication.
Protein Description As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, ribosomal RNA processing and miRNA processing, as well as transcription regulation. Regulates the alternative splicing of exons exhibiting specific features. [PubMed: 12138182]
Protein Sequence MPTGFVAPILCVLLPSPTREAATVASATGDSASERESAAPAAAPTAEAPPPSVVTRPEPQALPSPAIRAPLPDLYPFGTMRGGGFGDRDRDRDRGGFGARGGGGLPPKKFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELIKVLEEANQAINPKLMQLVDHRGGGGGGGGRSRYRTTSSANNPNLMYQDECDRRLRGVKDGGRRDSASYRDRSETDRAGYANGSGYGSPNSAFGAQAGQYTYGQGTYGAAAYGTSSYTAQEYGAGTYGASSTTSTGRSSQSSSQQFSGIGRSGQQPQPLMSQQFAQPPGATNMIGYMGQTAYQYPPPPPPPPPSRK
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
3Phosphorylation-----MPTGFVAPIL
-----CCCCCCCEEE		41.7924043423
16PhosphorylationILCVLLPSPTREAAT
EEEEECCCCCHHHHH		38.5824043423
18PhosphorylationCVLLPSPTREAATVA
EEECCCCCHHHHHHH		45.5427050516
37PhosphorylationDSASERESAAPAAAP
CCHHHHHHCCCCCCC		35.6324732914
42 (in isoform 1)Ubiquitination-16.9621890473
42 (in isoform 2)Ubiquitination-16.9621890473
42 (in isoform 3)Ubiquitination-16.9621890473
45PhosphorylationAAPAAAPTAEAPPPS
CCCCCCCCCCCCCCC		32.1930243723
50 (in isoform 1)Sumoylation-40.63-
50 (in isoform 1)Ubiquitination-40.6321890473
50 (in isoform 2)Ubiquitination-40.6321890473
50 (in isoform 3)Ubiquitination-40.6321890473
52O-linked_GlycosylationTAEAPPPSVVTRPEP
CCCCCCCCCCCCCCC		34.6930059200
52PhosphorylationTAEAPPPSVVTRPEP
CCCCCCCCCCCCCCC		34.6930266825
53 (in isoform 1)Ubiquitination-6.6821890473
53 (in isoform 2)Ubiquitination-6.6821890473
53 (in isoform 3)Ubiquitination-6.6821890473
55O-linked_GlycosylationAPPPSVVTRPEPQAL
CCCCCCCCCCCCCCC		38.0530059200
55PhosphorylationAPPPSVVTRPEPQAL
CCCCCCCCCCCCCCC		38.0530266825
64O-linked_GlycosylationPEPQALPSPAIRAPL
CCCCCCCCCCCCCCC		28.0130059200
64PhosphorylationPEPQALPSPAIRAPL
CCCCCCCCCCCCCCC		28.0129255136
68MethylationALPSPAIRAPLPDLY
CCCCCCCCCCCCCCC		32.05-
75PhosphorylationRAPLPDLYPFGTMRG
CCCCCCCCCCCCCCC		12.1428857561
79PhosphorylationPDLYPFGTMRGGGFG
CCCCCCCCCCCCCCC		12.2228555341
81MethylationLYPFGTMRGGGFGDR
CCCCCCCCCCCCCCC		40.20-
88MethylationRGGGFGDRDRDRDRG
CCCCCCCCCCCCCCC		41.04-
94MethylationDRDRDRDRGGFGARG
CCCCCCCCCCCCCCC		48.29-
100MethylationDRGGFGARGGGGLPP
CCCCCCCCCCCCCCC		44.67-
108AcetylationGGGGLPPKKFGNPGE
CCCCCCCHHHCCHHH		59.8120663877
109AcetylationGGGLPPKKFGNPGER
CCCCCCHHHCCHHHH		65.3620663877
116MethylationKFGNPGERLRKKKWD
HHCCHHHHHHHCCCC		45.79-
1212-HydroxyisobutyrylationGERLRKKKWDLSELP
HHHHHHCCCCHHHCC		49.31-
121AcetylationGERLRKKKWDLSELP
HHHHHHCCCCHHHCC		49.3120663877
121UbiquitinationGERLRKKKWDLSELP
HHHHHHCCCCHHHCC		49.31-
121 (in isoform 4)Ubiquitination-49.3121890473
125PhosphorylationRKKKWDLSELPKFEK
HHCCCCHHHCCCCCC		34.3228555341
129SumoylationWDLSELPKFEKNFYV
CCHHHCCCCCCCEEC		77.95-
129AcetylationWDLSELPKFEKNFYV
CCHHHCCCCCCCEEC		77.9523236377
129SumoylationWDLSELPKFEKNFYV
CCHHHCCCCCCCEEC		77.9525114211
129UbiquitinationWDLSELPKFEKNFYV
CCHHHCCCCCCCEEC		77.9519608861
129 (in isoform 4)Ubiquitination-77.9521890473
1322-HydroxyisobutyrylationSELPKFEKNFYVEHP
HHCCCCCCCEECCCH		56.33-
132AcetylationSELPKFEKNFYVEHP
HHCCCCCCCEECCCH		56.3325825284
132UbiquitinationSELPKFEKNFYVEHP
HHCCCCCCCEECCCH		56.33-
132 (in isoform 4)Ubiquitination-56.3321890473
135PhosphorylationPKFEKNFYVEHPEVA
CCCCCCEECCCHHHH		17.8328152594
143MethylationVEHPEVARLTPYEVD
CCCHHHHHCCCCCHH		44.25-
145PhosphorylationHPEVARLTPYEVDEL
CHHHHHCCCCCHHHH		20.4721815630
147PhosphorylationEVARLTPYEVDELRR
HHHHCCCCCHHHHHH		24.2928152594
153MethylationPYEVDELRRKKEITV
CCCHHHHHHCCCEEE		46.45-
181PhosphorylationHHANFPQYVMDVLMD
ECCCCHHHHHHHHHH		9.66-
200PhosphorylationEPTPIQCQGFPLALS
CCCCCCCCCCCEEEC		39.9418083107
205 (in isoform 1)Ubiquitination-10.4221890473
205 (in isoform 2)Ubiquitination-10.4221890473
205 (in isoform 3)Ubiquitination-10.4221890473
217PhosphorylationDMVGIAQTGSGKTLA
CEEEEEECCCCHHHH		25.0520068231
219PhosphorylationVGIAQTGSGKTLAYL
EEEEECCCCHHHHHH		40.2720068231
242PhosphorylationHQPYLERGDGPICLV
CCCCCCCCCCCEEEE		34.5516097034
247GlutathionylationERGDGPICLVLAPTR
CCCCCCEEEEEECHH		2.1222555962
267PhosphorylationVQQVADDYGKCSRLK
HHHHHHHHCCCHHCC		21.0228152594
269AcetylationQVADDYGKCSRLKST
HHHHHHCCCHHCCCC		23.8625953088
269UbiquitinationQVADDYGKCSRLKST
HHHHHHCCCHHCCCC		23.86-
270GlutathionylationVADDYGKCSRLKSTC
HHHHHCCCHHCCCCE		2.1922555962
274MethylationYGKCSRLKSTCIYGG
HCCCHHCCCCEEECC		42.48-
274UbiquitinationYGKCSRLKSTCIYGG
HCCCHHCCCCEEECC		42.48-
275PhosphorylationGKCSRLKSTCIYGGA
CCCHHCCCCEEECCC		32.8628152594
276PhosphorylationKCSRLKSTCIYGGAP
CCHHCCCCEEECCCC		11.0128152594
277GlutathionylationCSRLKSTCIYGGAPK
CHHCCCCEEECCCCC		2.6622555962
277S-nitrosylationCSRLKSTCIYGGAPK
CHHCCCCEEECCCCC		2.662212679
279PhosphorylationRLKSTCIYGGAPKGP
HCCCCEEECCCCCCC		16.2027273156
282 (in isoform 1)Ubiquitination-9.7721890473
282 (in isoform 2)Ubiquitination-9.7721890473
282 (in isoform 3)Ubiquitination-9.7721890473
284UbiquitinationCIYGGAPKGPQIRDL
EEECCCCCCCCCCCH		80.72-
284 (in isoform 4)Ubiquitination-80.7221890473
298GlutathionylationLERGVEICIATPGRL
HHCCEEEEEECCCHH		0.8022555962
298S-palmitoylationLERGVEICIATPGRL
HHCCEEEEEECCCHH		0.8029575903
301PhosphorylationGVEICIATPGRLIDF
CEEEEEECCCHHHHH		13.3330266825
311PhosphorylationRLIDFLESGKTNLRR
HHHHHHHHCCCCHHH		47.9721712546
3132-HydroxyisobutyrylationIDFLESGKTNLRRCT
HHHHHHCCCCHHHCC		43.44-
313AcetylationIDFLESGKTNLRRCT
HHHHHHCCCCHHHCC		43.4425953088
313MalonylationIDFLESGKTNLRRCT
HHHHHHCCCCHHHCC		43.4426320211
313UbiquitinationIDFLESGKTNLRRCT
HHHHHHCCCCHHHCC		43.44-
319GlutathionylationGKTNLRRCTYLVLDE
CCCCHHHCCEEEEEH		2.0722555962
320PhosphorylationKTNLRRCTYLVLDEA
CCCHHHCCEEEEEHH		20.3428152594
321PhosphorylationTNLRRCTYLVLDEAD
CCHHHCCEEEEEHHH		9.8428152594
330SulfoxidationVLDEADRMLDMGFEP
EEEHHHHHHHCCCHH		3.7128183972
333SulfoxidationEADRMLDMGFEPQIR
HHHHHHHCCCHHHHH		6.1228183972
340MethylationMGFEPQIRKIVDQIR
CCCHHHHHHHHHHHC		19.87-
341AcetylationGFEPQIRKIVDQIRP
CCHHHHHHHHHHHCC		49.0321689455
341UbiquitinationGFEPQIRKIVDQIRP
CCHHHHHHHHHHHCC		49.03-
350MethylationVDQIRPDRQTLMWSA
HHHHCCCCCEEEEEC		33.78-
356PhosphorylationDRQTLMWSATWPKEV
CCCEEEEECCCCHHH		11.23-
361UbiquitinationMWSATWPKEVRQLAE
EEECCCCHHHHHHHH		61.47-
361 (in isoform 4)Ubiquitination-61.4721890473
4172-HydroxyisobutyrylationMEEIMAEKENKTIIF
HHHHHHHHCCCEEEE		57.98-
417AcetylationMEEIMAEKENKTIIF
HHHHHHHHCCCEEEE		57.9825953088
417UbiquitinationMEEIMAEKENKTIIF
HHHHHHHHCCCEEEE		57.98-
4202-HydroxyisobutyrylationIMAEKENKTIIFVET
HHHHHCCCEEEEEEC		42.04-
420UbiquitinationIMAEKENKTIIFVET
HHHHHCCCEEEEEEC		42.04-
427PhosphorylationKTIIFVETKRRCDDL
CEEEEEECCCCCHHH		25.2520068231
4282-HydroxyisobutyrylationTIIFVETKRRCDDLT
EEEEEECCCCCHHHH		25.08-
428AcetylationTIIFVETKRRCDDLT
EEEEEECCCCCHHHH		25.0825953088
435PhosphorylationKRRCDDLTRRMRRDG
CCCCHHHHHHHHHCC		24.1922210691
436 (in isoform 3)Ubiquitination-37.3821890473
438 (in isoform 2)Ubiquitination-3.5721890473
444PhosphorylationRMRRDGWPAMCIHGD
HHHHCCCCCEEECCC		18.6916964243
447GlutathionylationRDGWPAMCIHGDKSQ
HCCCCCEEECCCCCC		1.9522555962
449 (in isoform 3)Ubiquitination-33.2121890473
451 (in isoform 2)Ubiquitination-33.0221890473
452AcetylationAMCIHGDKSQPERDW
CEEECCCCCCCHHHH		56.4325953088
452UbiquitinationAMCIHGDKSQPERDW
CEEECCCCCCCHHHH		56.43-
468SumoylationLNEFRSGKAPILIAT
HHHHHCCCCCEEEEE		52.84-
468AcetylationLNEFRSGKAPILIAT
HHHHHCCCCCEEEEE		52.8425953088
468UbiquitinationLNEFRSGKAPILIAT
HHHHHCCCCCEEEEE		52.84-
468 (in isoform 3)Ubiquitination-52.8421890473
470 (in isoform 2)Ubiquitination-25.9621890473
475PhosphorylationKAPILIATDVASRGL
CCCEEEEECHHHCCC		24.8229255136
479PhosphorylationLIATDVASRGLDVED
EEEECHHHCCCCHHH		27.0829255136
480MethylationIATDVASRGLDVEDV
EEECHHHCCCCHHHE		39.70-
488 (in isoform 3)Phosphorylation-46.35-
493PhosphorylationDVKFVINYDYPNSSE
HEEEEEECCCCCCCH		13.01-
494 (in isoform 3)Phosphorylation-48.1825849741
498PhosphorylationINYDYPNSSEDYVHR
EECCCCCCCHHHHHH		30.51-
499PhosphorylationNYDYPNSSEDYVHRI
ECCCCCCCHHHHHHH		40.92-
502PhosphorylationYPNSSEDYVHRIGRT
CCCCCHHHHHHHHCC		8.29-
505MethylationSSEDYVHRIGRTARS
CCHHHHHHHHCCCCC		24.02-
515UbiquitinationRTARSTNKGTAYTFF
CCCCCCCCCCEEEEE		58.70-
515 (in isoform 4)Ubiquitination-58.7021890473
517PhosphorylationARSTNKGTAYTFFTP
CCCCCCCCEEEEECC		20.3527251275
519PhosphorylationSTNKGTAYTFFTPGN
CCCCCCEEEEECCCC		12.1528152594
520PhosphorylationTNKGTAYTFFTPGNL
CCCCCEEEEECCCCH		15.1427251275
523PhosphorylationGTAYTFFTPGNLKQA
CCEEEEECCCCHHHH		26.5425159151
528AcetylationFFTPGNLKQARELIK
EECCCCHHHHHHHHH		46.0025953088
528SumoylationFFTPGNLKQARELIK
EECCCCHHHHHHHHH		46.0028112733
528UbiquitinationFFTPGNLKQARELIK
EECCCCHHHHHHHHH		46.00-
528 (in isoform 4)Ubiquitination-46.0021890473
535UbiquitinationKQARELIKVLEEANQ
HHHHHHHHHHHHHHH		54.08-
5472-HydroxyisobutyrylationANQAINPKLMQLVDH
HHHHHCHHHHHHHCC		52.70-
547AcetylationANQAINPKLMQLVDH
HHHHHCHHHHHHHCC		52.7025953088
547UbiquitinationANQAINPKLMQLVDH
HHHHHCHHHHHHHCC		52.70-
547 (in isoform 4)Ubiquitination-52.7021890473
549SulfoxidationQAINPKLMQLVDHRG
HHHCHHHHHHHCCCC		3.4621406390
555MethylationLMQLVDHRGGGGGGG
HHHHHCCCCCCCCCC		40.77-
564MethylationGGGGGGGRSRYRTTS
CCCCCCCCCCCCCCC		22.64-
565PhosphorylationGGGGGGRSRYRTTSS
CCCCCCCCCCCCCCC		36.62-
567PhosphorylationGGGGRSRYRTTSSAN
CCCCCCCCCCCCCCC		17.35-
567PhosphorylationGGGGRSRYRTTSSAN
CCCCCCCCCCCCCCC		17.3521945579
568MethylationGGGRSRYRTTSSANN
CCCCCCCCCCCCCCC		30.34-
569PhosphorylationGGRSRYRTTSSANNP
CCCCCCCCCCCCCCC		23.3021945579
570PhosphorylationGRSRYRTTSSANNPN
CCCCCCCCCCCCCCC		16.2221945579
571PhosphorylationRSRYRTTSSANNPNL
CCCCCCCCCCCCCCC		27.17-
571PhosphorylationRSRYRTTSSANNPNL
CCCCCCCCCCCCCCC		27.1721945579
572PhosphorylationSRYRTTSSANNPNLM
CCCCCCCCCCCCCCC		32.6821945579
573PhosphorylationRYRTTSSANNPNLMY
CCCCCCCCCCCCCCC		21.4225849741
573PhosphorylationRYRTTSSANNPNLMY
CCCCCCCCCCCCCCC		21.4225849741
574PhosphorylationYRTTSSANNPNLMYQ
CCCCCCCCCCCCCCC		67.45-
574PhosphorylationYRTTSSANNPNLMYQ
CCCCCCCCCCCCCCC		67.45-
580PhosphorylationANNPNLMYQDECDRR
CCCCCCCCCCHHHHH		18.9121945579
584GlutathionylationNLMYQDECDRRLRGV
CCCCCCHHHHHHCCC		7.1122555962
592MethylationDRRLRGVKDGGRRDS
HHHHCCCCCCCCCCC		54.18-
593PhosphorylationRRLRGVKDGGRRDSA
HHHCCCCCCCCCCCC		63.4717525332
597PhosphorylationGVKDGGRRDSASYRD
CCCCCCCCCCCHHCC		45.5717525332
599PhosphorylationKDGGRRDSASYRDRS
CCCCCCCCCHHCCCC		19.8026846344
601PhosphorylationGGRRDSASYRDRSET
CCCCCCCHHCCCCHH		25.3423401153
602PhosphorylationGRRDSASYRDRSETD
CCCCCCHHCCCCHHC		19.0927461979
605MethylationDSASYRDRSETDRAG
CCCHHCCCCHHCCCC		27.65-
606PhosphorylationSASYRDRSETDRAGY
CCHHCCCCHHCCCCC		49.4927251275
619PhosphorylationGYANGSGYGSPNSAF
CCCCCCCCCCCCCCC		19.0026074081
621PhosphorylationANGSGYGSPNSAFGA
CCCCCCCCCCCCCCC		16.6626074081
624PhosphorylationSGYGSPNSAFGAQAG
CCCCCCCCCCCCCCC		28.4926074081
655PhosphorylationSSYTAQEYGAGTYGA
CCEEEHHHCCCCCCC		10.53-
660PhosphorylationQEYGAGTYGASSTTS
HHHCCCCCCCCCCCC		15.13-
663O-linked_GlycosylationGAGTYGASSTTSTGR
CCCCCCCCCCCCCCC		24.6930059200
665O-linked_GlycosylationGTYGASSTTSTGRSS
CCCCCCCCCCCCCCC		23.4430059200
666O-linked_GlycosylationTYGASSTTSTGRSSQ
CCCCCCCCCCCCCCC		26.6630059200
667O-linked_GlycosylationYGASSTTSTGRSSQS
CCCCCCCCCCCCCCC		29.0230059200
668O-linked_GlycosylationGASSTTSTGRSSQSS
CCCCCCCCCCCCCCC		34.2330059200
671O-linked_GlycosylationSTTSTGRSSQSSSQQ
CCCCCCCCCCCCCCC		33.7930059200
671PhosphorylationSTTSTGRSSQSSSQQ
CCCCCCCCCCCCCCC		33.7923401153
672O-linked_GlycosylationTTSTGRSSQSSSQQF
CCCCCCCCCCCCCCC		32.4930059200
672PhosphorylationTTSTGRSSQSSSQQF
CCCCCCCCCCCCCCC		32.4917525332
674O-linked_GlycosylationSTGRSSQSSSQQFSG
CCCCCCCCCCCCCCC		33.6330059200
674PhosphorylationSTGRSSQSSSQQFSG
CCCCCCCCCCCCCCC		33.6317525332
675O-linked_GlycosylationTGRSSQSSSQQFSGI
CCCCCCCCCCCCCCC		25.2430059200
675PhosphorylationTGRSSQSSSQQFSGI
CCCCCCCCCCCCCCC		25.2421955146
676O-linked_GlycosylationGRSSQSSSQQFSGIG
CCCCCCCCCCCCCCC		32.9930059200
676PhosphorylationGRSSQSSSQQFSGIG
CCCCCCCCCCCCCCC		32.9917525332
680PhosphorylationQSSSQQFSGIGRSGQ
CCCCCCCCCCCCCCC		25.7621712546
684MethylationQQFSGIGRSGQQPQP
CCCCCCCCCCCCCCC		35.3824129315
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 DDX17_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX17_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 DDX17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WBP11_HUMANWBP11physical
16189514
LNX1_HUMANLNX1physical
16189514
HDAC1_HUMANHDAC1physical
15298701
RU17_HUMANSNRNP70physical
12193588
KAT2B_HUMANKAT2Bphysical
17226766
EP300_HUMANEP300physical
17226766
CBP_HUMANCREBBPphysical
17226766
ESR1_HUMANESR1physical
19995069
EP300_HUMANEP300physical
19995069
DDX5_HUMANDDX5physical
19995069
DDX17_HUMANDDX17physical
19995069
HDAC1_HUMANHDAC1physical
19995069
HDAC2_HUMANHDAC2physical
19995069
HDAC3_HUMANHDAC3physical
19995069
A4_HUMANAPPphysical
21832049
DDX5_HUMANDDX5physical
22939629
DHX9_HUMANDHX9physical
22939629
SRSF1_HUMANSRSF1physical
22939629
U5S1_HUMANEFTUD2physical
22939629
SRSF3_HUMANSRSF3physical
22939629
SF3A1_HUMANSF3A1physical
22939629
DSRAD_HUMANADARphysical
22939629
RBP2_HUMANRANBP2physical
22939629
IF5A1_HUMANEIF5Aphysical
22939629
SF3B4_HUMANSF3B4physical
22365833
U2AF2_HUMANU2AF2physical
22365833
SF01_HUMANSF1physical
22365833
WBP11_HUMANWBP11physical
22365833
DDX17_HUMANDDX17physical
22365833
DDX5_HUMANDDX5physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
RBM4_HUMANRBM4physical
22365833
HNRH3_HUMANHNRNPH3physical
22365833
LSM1_HUMANLSM1physical
22863883
KPRA_HUMANPRPSAP1physical
22863883
RBM15_HUMANRBM15physical
25416956
EP300_HUMANEP300physical
20663877
ESR1_HUMANESR1physical
20663877
ATX2_HUMANATXN2physical
26344197
ATX2L_HUMANATXN2Lphysical
26344197
CPSF6_HUMANCPSF6physical
26344197
HNRPL_HUMANHNRNPLphysical
26344197
ILK_HUMANILKphysical
26344197
NOSIP_HUMANNOSIPphysical
26344197
PARVA_HUMANPARVAphysical
26344197
PLEC_HUMANPLECphysical
26344197
PLPHP_HUMANPROSCphysical
26344197
SYQ_HUMANQARSphysical
26344197
SFPQ_HUMANSFPQphysical
26344197
SMRC2_HUMANSMARCC2physical
26344197
YLPM1_HUMANYLPM1physical
26344197
FNBP4_HUMANFNBP4physical
28514442
DDX5_HUMANDDX5physical
28514442
NIF3L_HUMANNIF3L1physical
28514442
AMPD2_HUMANAMPD2physical
28514442
PP1R7_HUMANPPP1R7physical
27173435
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX17_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-676, ANDMASS SPECTROMETRY.
"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 THR-523, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Sumoylation of p68 and p72 RNA helicases affects protein stabilityand transactivation potential.";
Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R.;
Biochemistry 49:1-10(2010).
Cited for: SUMOYLATION AT LYS-129, AND MUTAGENESIS OF LYS-129.

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