DHX16_HUMAN - dbPTM
DHX16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX16_HUMAN
UniProt AC O60231
Protein Name Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
Gene Name DHX16
Organism Homo sapiens (Human).
Sequence Length 1041
Subcellular Localization Nucleus . Nucleus, nucleoplasm .
Protein Description Involved in pre-mRNA splicing. Contributes to pre-mRNA splicing after spliceosome formation and prior to the first transesterification reaction..
Protein Sequence MATPAGLERWVQDELHSVLGLSERHVAQFLIGTAQRCTSAEEFVQRLRDTDTLDLSGPARDFALRLWNKVPRKAVVEKPARAAEREARALLEKNRSYRLLEDSEESSEETVSRAGSSLQKKRKKRKHLRKKREEEEEEEASEKGKKKTGGSKQQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDRCRRLGSKIRELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNSIFYRPKDKVVHADNARVNFFLPGGDHLVLLNVYTQWAESGYSSQWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVRKAITAGYFYHTARLTRSGYRTVKQQQTVFIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAPHYYKAKELEDPHAKKMPKKIGKTREELG
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-----MATPAGLERW
-----CCCCHHHHHH		26.0722199227
52PhosphorylationQRLRDTDTLDLSGPA
HHHHCCCCCCCCCCH		25.0230087585
56PhosphorylationDTDTLDLSGPARDFA
CCCCCCCCCCHHHHH		42.2628674419
65MethylationPARDFALRLWNKVPR
CHHHHHHHHHHCCCH		33.94-
78UbiquitinationPRKAVVEKPARAAER
CHHHHCCCHHHHHHH		32.16-
78AcetylationPRKAVVEKPARAAER
CHHHHCCCHHHHHHH		32.1623749302
93UbiquitinationEARALLEKNRSYRLL
HHHHHHHHCHHHHCC		58.59-
103PhosphorylationSYRLLEDSEESSEET
HHHCCCCCCCCCHHH		33.6129255136
106PhosphorylationLLEDSEESSEETVSR
CCCCCCCCCHHHHHH		38.7129255136
107PhosphorylationLEDSEESSEETVSRA
CCCCCCCCHHHHHHH		42.6119664994
110PhosphorylationSEESSEETVSRAGSS
CCCCCHHHHHHHHHH		21.5230266825
112PhosphorylationESSEETVSRAGSSLQ
CCCHHHHHHHHHHHH		24.6722167270
116PhosphorylationETVSRAGSSLQKKRK
HHHHHHHHHHHHHHH		27.2220068231
117PhosphorylationTVSRAGSSLQKKRKK
HHHHHHHHHHHHHHH		33.6220068231
141PhosphorylationEEEEEEASEKGKKKT
HHHHHHHHHHCCCCC		43.0230576142
143AcetylationEEEEASEKGKKKTGG
HHHHHHHHCCCCCCC		73.8026051181
148PhosphorylationSEKGKKKTGGSKQQT
HHHCCCCCCCCCCCC		56.5126074081
151PhosphorylationGKKKTGGSKQQTEKP
CCCCCCCCCCCCCCC		28.7426074081
155PhosphorylationTGGSKQQTEKPESED
CCCCCCCCCCCCCHH		43.4130266825
160PhosphorylationQQTEKPESEDEWERT
CCCCCCCCHHHHHHH		59.9022167270
167PhosphorylationSEDEWERTERERLQD
CHHHHHHHHHHHHHH		28.0723403867
202AcetylationNVLERSDKKAYEEAQ
HHHHHHHHHHHHHHH		40.3220167786
203AcetylationVLERSDKKAYEEAQK
HHHHHHHHHHHHHHH		62.2820167786
205PhosphorylationERSDKKAYEEAQKRL
HHHHHHHHHHHHHHH		24.15-
210AcetylationKAYEEAQKRLKMAEE
HHHHHHHHHHHHHHH		67.7425953088
228AcetylationAMVPELRKKSRREYL
HCHHHHHHHHHHHHH		68.6610534025
291UbiquitinationRAAGEQEKLEATNRY
HHHCHHHHHHHHCCC		51.85-
304PhosphorylationRYHMPKETRGQPARA
CCCCCHHHCCCCCCH		46.3430576142
338PhosphorylationEARLGAASLKFGARD
HHHHHHHHHHHCCCC		31.4023186163
340AcetylationRLGAASLKFGARDAA
HHHHHHHHHCCCCCC		38.9825953088
340UbiquitinationRLGAASLKFGARDAA
HHHHHHHHHCCCCCC		38.98-
348PhosphorylationFGARDAASQEPKYQL
HCCCCCCCCCCCEEE		36.4825159151
369PhosphorylationTIEFVRATQLQGDEE
HHHHHHHHHCCCCCC		21.1722817901
389UbiquitinationTSTQAQQKESIQAVR
CCHHHHHHHHHHHHH		41.1521906983
391PhosphorylationTQAQQKESIQAVRRS
HHHHHHHHHHHHHHH		27.3423532336
444UbiquitinationFEEGYTNKGMKIACT
CCCCCCCCCCEEEEC		53.21-
447UbiquitinationGYTNKGMKIACTQPR
CCCCCCCEEEECCHH		35.50-
460PhosphorylationPRRVAAMSVAARVAR
HHHHHHHHHHHHHHH		12.13-
480PhosphorylationLGNEVGYSIRFEDCT
CCCCCCEEEEEECCC		11.0224719451
537UbiquitinationDILFGLIKDVARFRP
HHHHHHHHHHHHHCH		51.71-
552PhosphorylationELKVLVASATMDTAR
HHHHHEEECCCCHHH		19.4520068231
554PhosphorylationKVLVASATMDTARFS
HHHEEECCCCHHHHH		17.0620068231
555SulfoxidationVLVASATMDTARFST
HHEEECCCCHHHHHH		4.2721406390
557PhosphorylationVASATMDTARFSTFF
EEECCCCHHHHHHCC		14.6520068231
663PhosphorylationQARIFQPTPPGARKV
HCHHCCCCCCCCCEE		31.19-
674PhosphorylationARKVVVATNIAETSL
CCEEEEEEEECCCEE		18.6230576142
679PhosphorylationVATNIAETSLTIEGI
EEEEECCCEEEEEEE		21.7330576142
699PhosphorylationPGFCKQKSYNPRTGM
CCCCCCCCCCCCCCC		27.8722468782
700PhosphorylationGFCKQKSYNPRTGME
CCCCCCCCCCCCCCE		35.9030206219
704PhosphorylationQKSYNPRTGMESLTV
CCCCCCCCCCEEEEE		41.9830206219
706SulfoxidationSYNPRTGMESLTVTP
CCCCCCCCEEEEECC		2.9021406390
708PhosphorylationNPRTGMESLTVTPCS
CCCCCCEEEEECCCC		22.0521888424
712PhosphorylationGMESLTVTPCSKASA
CCEEEEECCCCHHCC		17.2225159151
715PhosphorylationSLTVTPCSKASANQR
EEEECCCCHHCCCCC		32.2422468782
716UbiquitinationLTVTPCSKASANQRA
EEECCCCHHCCCCCC		53.75-
718PhosphorylationVTPCSKASANQRAGR
ECCCCHHCCCCCCCC		31.3330206219
733UbiquitinationAGRVAAGKCFRLYTA
CHHHHHHHHHHHHHH		26.02-
733AcetylationAGRVAAGKCFRLYTA
CHHHHHHHHHHHHHH		26.0225953088
814UbiquitinationELTTSGRKMAELPVD
HCCCCCCCCCCCCCC		46.09-
826UbiquitinationPVDPMLSKMILASEK
CCCHHHHHHHHHCCC		26.46-
860AcetylationIFYRPKDKVVHADNA
CEECCCCCEEECCCC		52.8925953088
944PhosphorylationIRVRKAITAGYFYHT
HHHHHHHHCCCCHHH		20.9128348404
947PhosphorylationRKAITAGYFYHTARL
HHHHHCCCCHHHCCC		9.8628348404
949PhosphorylationAITAGYFYHTARLTR
HHHCCCCHHHCCCCC		6.9728348404
951PhosphorylationTAGYFYHTARLTRSG
HCCCCHHHCCCCCCC		11.3328348404
955PhosphorylationFYHTARLTRSGYRTV
CHHHCCCCCCCCCCC		19.7528348404
967PhosphorylationRTVKQQQTVFIHPNS
CCCEEEEEEEECCCC		17.0424043423
974PhosphorylationTVFIHPNSSLFEQQP
EEEECCCCHHHCCCC		32.6324043423
975PhosphorylationVFIHPNSSLFEQQPR
EEECCCCHHHCCCCH		43.6624043423
986PhosphorylationQQPRWLLYHELVLTT
CCCHHHHHHHHHHHH		7.3524043423
992PhosphorylationLYHELVLTTKEFMRQ
HHHHHHHHHHHHHHH		28.4824043423
993PhosphorylationYHELVLTTKEFMRQV
HHHHHHHHHHHHHHH		25.1524043423
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 DHX16_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX16_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 DHX16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNR27_HUMANSNRNP27physical
2479028
SNR40_HUMANSNRNP40physical
2479028
A4_HUMANAPPphysical
21832049
LSM6_HUMANLSM6physical
22939629
LSM2_HUMANLSM2physical
22939629
LSM5_HUMANLSM5physical
22939629
GABP1_HUMANGABPB1physical
22939629
GON4L_HUMANGON4Lphysical
22939629
GCC2_HUMANGCC2physical
22939629
MI4GD_HUMANMIF4GDphysical
22939629
PYRD1_HUMANPYROXD1physical
22939629
TCEA2_HUMANTCEA2physical
22939629
EHD2_HUMANEHD2physical
22939629
NAA40_HUMANNAA40physical
22939629
METH_HUMANMTRphysical
22939629
ERF3A_HUMANGSPT1physical
22939629
WDR44_HUMANWDR44physical
22939629
HELQ_HUMANHELQphysical
22939629
SF3B2_HUMANSF3B2physical
22365833
SYF1_HUMANXAB2physical
22365833
PRP16_HUMANDHX38physical
22365833
DGC14_HUMANDGCR14physical
22365833
GPKOW_HUMANGPKOWphysical
22365833
GPKOW_HUMANGPKOWphysical
25296192
KC1E_HUMANCSNK1Ephysical
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 DHX16_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-103, AND MASSSPECTROMETRY.
"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-103; SER-106 ANDSER-107, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-107, ANDMASS 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-103; SER-106 ANDSER-107, 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-103 AND SER-106, ANDMASS SPECTROMETRY.
"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-103; SER-106; SER-107AND SER-160, AND MASS SPECTROMETRY.
"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 SER-103, AND MASSSPECTROMETRY.

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