DDX23_HUMAN - dbPTM
DDX23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX23_HUMAN
UniProt AC Q9BUQ8
Protein Name Probable ATP-dependent RNA helicase DDX23
Gene Name DDX23
Organism Homo sapiens (Human).
Sequence Length 820
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation..
Protein Sequence MAGELADKKDRDASPSKEERKRSRTPDRERDRDRDRKSSPSKDRKRHRSRDRRRGGSRSRSRSRSKSAERERRHKERERDKERDRNKKDRDRDKDGHRRDKDRKRSSLSPGRGKDFKSRKDRDSKKDEEDEHGDKKPKAQPLSLEELLAKKKAEEEAEAKPKFLSKAEREAEALKRRQQEVEERQRMLEEERKKRKQFQDLGRKMLEDPQERERRERRERMERETNGNEDEEGRQKIREEKDKSKELHAIKERYLGGIKKRRRTRHLNDRKFVFEWDASEDTSIDYNPLYKERHQVQLLGRGFIAGIDLKQQKREQSRFYGDLMEKRRTLEEKEQEEARLRKLRKKEAKQRWDDRHWSQKKLDEMTDRDWRIFREDYSITTKGGKIPNPIRSWKDSSLPPHILEVIDKCGYKEPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEESDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEHMPVSNQKPDTDEAEDPEKMLANFESGKHKYRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAGKPHERVEQKVFLMSESEKRKKLLAILEQGFDPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVVNYDMAKNIEDYIHRIGRTGRAGKSGVAITFLTKEDSAVFYELKQAILESPVSSCPPELANHPDAQHKPGTILTKKRREETIFA
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
14PhosphorylationDKKDRDASPSKEERK
CCCCCCCCCCHHHHH		33.7129255136
16PhosphorylationKDRDASPSKEERKRS
CCCCCCCCHHHHHHH		50.6430266825
23PhosphorylationSKEERKRSRTPDRER
CHHHHHHHCCCCHHH		43.4720068231
25PhosphorylationEERKRSRTPDRERDR
HHHHHHCCCCHHHHH		30.6820068231
38PhosphorylationDRDRDRKSSPSKDRK
HHHCCCCCCCCHHHH		48.6622210691
39PhosphorylationRDRDRKSSPSKDRKR
HHCCCCCCCCHHHHH		35.9127422710
41PhosphorylationRDRKSSPSKDRKRHR
CCCCCCCCHHHHHHH		49.4926074081
67PhosphorylationRSRSRSKSAERERRH
HHHHHHHHHHHHHHH		36.2922817900
106PhosphorylationRDKDRKRSSLSPGRG
CHHHHCHHCCCCCCC		38.3722167270
107PhosphorylationDKDRKRSSLSPGRGK
HHHHCHHCCCCCCCC		36.5822167270
109PhosphorylationDRKRSSLSPGRGKDF
HHCHHCCCCCCCCCC		27.5322167270
124PhosphorylationKSRKDRDSKKDEEDE
CCCCCCCCCCCCCCC		42.3630576142
136AcetylationEDEHGDKKPKAQPLS
CCCCCCCCCCCCCCC		57.3930588055
138AcetylationEHGDKKPKAQPLSLE
CCCCCCCCCCCCCHH		69.4130588061
143PhosphorylationKPKAQPLSLEELLAK
CCCCCCCCHHHHHHH		40.1825849741
150AcetylationSLEELLAKKKAEEEA
CHHHHHHHHHHHHHH		55.5730588067
1502-HydroxyisobutyrylationSLEELLAKKKAEEEA
CHHHHHHHHHHHHHH		55.57-
150UbiquitinationSLEELLAKKKAEEEA
CHHHHHHHHHHHHHH		55.57-
160AcetylationAEEEAEAKPKFLSKA
HHHHHHHCHHHHHHH		40.0026051181
1662-HydroxyisobutyrylationAKPKFLSKAEREAEA
HCHHHHHHHHHHHHH		57.31-
196MalonylationEEERKKRKQFQDLGR
HHHHHHHHHHHHHHH		65.4326320211
205SulfoxidationFQDLGRKMLEDPQER
HHHHHHHHCCCHHHH		4.8321406390
251UbiquitinationSKELHAIKERYLGGI
HHHHHHHHHHHHCCH		36.60-
2592-HydroxyisobutyrylationERYLGGIKKRRRTRH
HHHHCCHHHHCCCCC		43.43-
264PhosphorylationGIKKRRRTRHLNDRK
CHHHHCCCCCCCCCC		22.19-
301MethylationHQVQLLGRGFIAGID
HHHHHHCCCEECCCC		36.50-
3102-HydroxyisobutyrylationFIAGIDLKQQKREQS
EECCCCHHHHHHHHH		47.11-
3262-HydroxyisobutyrylationFYGDLMEKRRTLEEK
HHHHHHHHHHCHHHH		32.96-
326UbiquitinationFYGDLMEKRRTLEEK
HHHHHHHHHHCHHHH		32.9621890473
326UbiquitinationFYGDLMEKRRTLEEK
HHHHHHHHHHCHHHH		32.9621890473
333AcetylationKRRTLEEKEQEEARL
HHHCHHHHHHHHHHH		56.1526051181
366PhosphorylationQKKLDEMTDRDWRIF
HHHHHHCCCCCHHHH		26.3226074081
377PhosphorylationWRIFREDYSITTKGG
HHHHHCCCEEEECCC		9.38-
378PhosphorylationRIFREDYSITTKGGK
HHHHCCCEEEECCCC		26.27-
380PhosphorylationFREDYSITTKGGKIP
HHCCCEEEECCCCCC		19.26-
381PhosphorylationREDYSITTKGGKIPN
HCCCEEEECCCCCCC		26.48-
394AcetylationPNPIRSWKDSSLPPH
CCCCCCCCCCCCCHH		49.3226051181
412AcetylationVIDKCGYKEPTPIQR
HHHHCCCCCCCCCCC		42.3625953088
437PhosphorylationDIIGVAETGSGKTAA
CEEEEEECCCCHHHH		27.2321406692
439PhosphorylationIGVAETGSGKTAAFL
EEEEECCCCHHHHHH		44.5321406692
470PhosphorylationEESDQGPYAIILAPT
CCCCCCCEEEEEECH		19.77-
477PhosphorylationYAIILAPTRELAQQI
EEEEEECHHHHHHHH		31.04-
490AcetylationQIEEETIKFGKPLGI
HHHHHHHHCCCCCCC		56.3225953088
507PhosphorylationVAVIGGISREDQGFR
EEEECCCCHHHCCCE		32.6520068231
508DimethylationAVIGGISREDQGFRL
EEECCCCHHHCCCEE		49.98-
517SulfoxidationDQGFRLRMGCEIVIA
HCCCEEECCCEEEEE		9.4821406390
541PhosphorylationENRYLVLSRCTYVVL
CCCHHHEECCCEEEE		20.1724719451
545PhosphorylationLVLSRCTYVVLDEAD
HHEECCCEEEEECHH		7.6828787133
579PhosphorylationVSNQKPDTDEAEDPE
CCCCCCCCCCCCCHH		44.24-
602PhosphorylationGKHKYRQTVMFTATM
CCCCEEEEEEEECCC		12.6323403867
606PhosphorylationYRQTVMFTATMPPAV
EEEEEEEECCCCHHH		11.7923403867
608PhosphorylationQTVMFTATMPPAVER
EEEEEECCCCHHHHH		27.4423403867
619PhosphorylationAVERLARSYLRRPAV
HHHHHHHHHHCCCEE		23.9423917254
620PhosphorylationVERLARSYLRRPAVV
HHHHHHHHHCCCEEE		9.9322817900
628PhosphorylationLRRPAVVYIGSAGKP
HCCCEEEEECCCCCC		7.9328152594
631PhosphorylationPAVVYIGSAGKPHER
CEEEEECCCCCCHHH		25.0428152594
634AcetylationVYIGSAGKPHERVEQ
EEECCCCCCHHHHHH		42.8126051181
642AcetylationPHERVEQKVFLMSES
CHHHHHHHEEECCHH		22.81132847
647PhosphorylationEQKVFLMSESEKRKK
HHHEEECCHHHHHHH		39.87-
6512-HydroxyisobutyrylationFLMSESEKRKKLLAI
EECCHHHHHHHHHHH		77.97-
682AcetylationKGCDVLAKSLEKMGY
CCHHHHHHHHHHCCC		51.9525953088
686AcetylationVLAKSLEKMGYNACT
HHHHHHHHCCCCEEE		42.8125953088
686SumoylationVLAKSLEKMGYNACT
HHHHHHHHCCCCEEE		42.8128112733
686UbiquitinationVLAKSLEKMGYNACT
HHHHHHHHCCCCEEE		42.81-
698UbiquitinationACTLHGGKGQEQREF
EEECCCCCCHHHHHH		63.11-
698AcetylationACTLHGGKGQEQREF
EEECCCCCCHHHHHH		63.1126051181
711UbiquitinationEFALSNLKAGAKDIL
HHHHHHHHCCCCEEE		49.37-
715MalonylationSNLKAGAKDILVATD
HHHHCCCCEEEEEEC		44.3726320211
715AcetylationSNLKAGAKDILVATD
HHHHCCCCEEEEEEC		44.3723749302
7152-HydroxyisobutyrylationSNLKAGAKDILVATD
HHHHCCCCEEEEEEC		44.37-
748PhosphorylationMAKNIEDYIHRIGRT
HHCCHHHHHHHHCCC		5.95-
755PhosphorylationYIHRIGRTGRAGKSG
HHHHHCCCCCCCCCC		26.30-
761PhosphorylationRTGRAGKSGVAITFL
CCCCCCCCCEEEEEE		37.2721712546
777PhosphorylationKEDSAVFYELKQAIL
CCCCHHHHHHHHHHH		17.4728152594
790PhosphorylationILESPVSSCPPELAN
HHHCCHHCCCHHHHC		30.77-
804AcetylationNHPDAQHKPGTILTK
CCCCCCCCCCCCCCC		32.8226051181
807PhosphorylationDAQHKPGTILTKKRR
CCCCCCCCCCCCCCC		22.72-
811SumoylationKPGTILTKKRREETI
CCCCCCCCCCCHHCC		40.6228112733
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 DDX23_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX23_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 DDX23_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3A3_HUMANSF3A3physical
22939629
PHF5A_HUMANPHF5Aphysical
22939629
THOC5_HUMANTHOC5physical
22939629
SNUT1_HUMANSART1physical
22939629
PURA_HUMANPURAphysical
22939629
PRPF3_HUMANPRPF3physical
26186194
RED_HUMANIKphysical
26186194
SNR40_HUMANSNRNP40physical
26186194
PRP6_HUMANPRPF6physical
26186194
U520_HUMANSNRNP200physical
26186194
PRP8_HUMANPRPF8physical
26186194
TFP11_HUMANTFIP11physical
26186194
U5S1_HUMANEFTUD2physical
26186194
PAXB1_HUMANPAXBP1physical
26186194
AAR2_HUMANAAR2physical
26186194
SNUT1_HUMANSART1physical
26186194
RSRC1_HUMANRSRC1physical
26186194
SMD2_HUMANSNRPD2physical
26186194
EAPP_HUMANEAPPphysical
26186194
CD2B2_HUMANCD2BP2physical
26186194
TXN4A_HUMANTXNL4Aphysical
26186194
ANM6_HUMANPRMT6physical
26186194
SMD1_HUMANSNRPD1physical
26186194
SPF27_HUMANBCAS2physical
26344197
U5S1_HUMANEFTUD2physical
26344197
HNRPR_HUMANHNRNPRphysical
26344197
PI42A_HUMANPIP4K2Aphysical
26344197
PI42B_HUMANPIP4K2Bphysical
26344197
PI42C_HUMANPIP4K2Cphysical
26344197
PRPF3_HUMANPRPF3physical
26344197
PRP6_HUMANPRPF6physical
26344197
PRP8_HUMANPRPF8physical
26344197
SNUT1_HUMANSART1physical
26344197
U520_HUMANSNRNP200physical
26344197
CD2B2_HUMANCD2BP2physical
28514442
EAPP_HUMANEAPPphysical
28514442
SNR40_HUMANSNRNP40physical
28514442
PRP6_HUMANPRPF6physical
28514442
RED_HUMANIKphysical
28514442
RSRC1_HUMANRSRC1physical
28514442
TFP11_HUMANTFIP11physical
28514442
ANM6_HUMANPRMT6physical
28514442
U520_HUMANSNRNP200physical
28514442
PAXB1_HUMANPAXBP1physical
28514442
PRP8_HUMANPRPF8physical
28514442
PRP4_HUMANPRPF4physical
28514442
SMD2_HUMANSNRPD2physical
28514442
SNUT1_HUMANSART1physical
28514442
AAR2_HUMANAAR2physical
28514442
TXN4A_HUMANTXNL4Aphysical
28514442
U5S1_HUMANEFTUD2physical
28514442
SMD1_HUMANSNRPD1physical
28514442
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 DDX23_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-107 AND SER-109, ANDMASS 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-14, 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-14; THR-25; SER-107 ANDSER-109, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.

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