DHX8_HUMAN - dbPTM
DHX8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX8_HUMAN
UniProt AC Q14562
Protein Name ATP-dependent RNA helicase DHX8
Gene Name DHX8
Organism Homo sapiens (Human).
Sequence Length 1220
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 11991638]
Protein Sequence MAVAVAMAGALIGSEPGPAEELAKLEYLSLVSKVCTELDNHLGINDKDLAEFVISLAEKNTTFDTFKASLVKNGAEFTDSLISNLLRLIQTMRPPAKPSTSKDPVVKPKTEKEKLKELFPVLCQPDNPSVRTMLDEDDVKVAVDVLKELEALMPSAAGQEKQRDAEHRDRTKKKKRSRSRDRNRDRDRDRERNRDRDHKRRHRSRSRSRSRTRERNKVKSRYRSRSRSQSPPKDRKDRDKYGERNLDRWRDKHVDRPPPEEPTIGDIYNGKVTSIMQFGCFVQLEGLRKRWEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSMKDVDQETGEDLNPNRRRNLVGETNEETSMRNPDRPTHLSLVSAPEVEDDSLERKRLTRISDPEKWEIKQMIAANVLSKEEFPDFDEETGILPKVDDEEDEDLEIELVEEEPPFLRGHTKQSMDMSPIKIVKNPDGSLSQAAMMQSALAKERRELKQAQREAEMDSIPMGLNKHWVDPLPDAEGRQIAANMRGIGMMPNDIPEWKKHAFGGNKASYGKKTQMSILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAVKFSQYFYEAPIFTIPGRTYPVEILYTKEPETDYLDASLITVMQIHLTEPPGDILVFLTGQEEIDTACEILYERMKSLGPDVPELIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVVTPISQAQAKQRAGRAGRTGPGKCYRLYTERAYRDEMLTTNVPEIQRTNLASTVLSLKAMGINDLLSFDFMDAPPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRPKDKQALADQKKAKFHQTEGDHLTLLAVYNSWKNNKFSNPWCYENFIQARSLRRAQDIRKQMLGIMDRHKLDVVSCGKSTVRVQKAICSGFFRNAAKKDPQEGYRTLIDQQVVYIHPSSALFNRQPEWVVYHELVLTTKEYMREVTTIDPRWLVEFAPAFFKVSDPTKLSKQKKQQRLEPLYNRYEEPNAWRISRAFRRR
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
2Acetylation------MAVAVAMAG
------CHHHHHHHH		14.85-
14PhosphorylationMAGALIGSEPGPAEE
HHHHHHCCCCCCHHH		33.3621406692
69PhosphorylationTFDTFKASLVKNGAE
CHHHHHHHHHHCCHH		34.0024719451
129PhosphorylationLCQPDNPSVRTMLDE
HCCCCCCCHHHCCCH		30.4125850435
140SumoylationMLDEDDVKVAVDVLK
CCCHHHHHHHHHHHH		31.3228112733
153SulfoxidationLKELEALMPSAAGQE
HHHHHHHCCCCCCHH		2.9621406390
177PhosphorylationRTKKKKRSRSRDRNR
HHHHHHHHHHHHHHH		43.4120068231
179PhosphorylationKKKKRSRSRDRNRDR
HHHHHHHHHHHHHHH		39.5220068231
204PhosphorylationDHKRRHRSRSRSRSR
HHHHHHHHHHHHHHH		28.6017081983
206PhosphorylationKRRHRSRSRSRSRTR
HHHHHHHHHHHHHHH		35.5417081983
222PhosphorylationRNKVKSRYRSRSRSQ
HHHHHHHHHHCCCCC		21.7429449344
224PhosphorylationKVKSRYRSRSRSQSP
HHHHHHHHCCCCCCC		26.1828060719
226PhosphorylationKSRYRSRSRSQSPPK
HHHHHHCCCCCCCCC		37.2123663014
228PhosphorylationRYRSRSRSQSPPKDR
HHHHCCCCCCCCCCC		35.9423663014
230PhosphorylationRSRSRSQSPPKDRKD
HHCCCCCCCCCCCCC		44.4023663014
241PhosphorylationDRKDRDKYGERNLDR
CCCCHHHHHHHHHHH		28.63-
263PhosphorylationRPPPEEPTIGDIYNG
CCCCCCCCCHHHCCC		40.65-
273PhosphorylationDIYNGKVTSIMQFGC
HHCCCEECEEEEEEE		18.93-
298PhosphorylationWEGLVHISELRREGR
HCCEEEHHHHHHCCC		18.7224719451
314PhosphorylationANVADVVSKGQRVKV
ECHHHHHCCCCEEEE		30.8029255136
327PhosphorylationKVKVLSFTGTKTSLS
EEEEEEEECCCEECC		40.33-
334PhosphorylationTGTKTSLSMKDVDQE
ECCCEECCCCCCCCC		24.4524719451
358PhosphorylationRRNLVGETNEETSMR
HCCCCCCCCCCCCCC		41.84-
362PhosphorylationVGETNEETSMRNPDR
CCCCCCCCCCCCCCC		22.96-
364SulfoxidationETNEETSMRNPDRPT
CCCCCCCCCCCCCCC		6.6521406390
374PhosphorylationPDRPTHLSLVSAPEV
CCCCCCEEEECCCCC		21.0828555341
377PhosphorylationPTHLSLVSAPEVEDD
CCCEEEECCCCCCCC		43.3230108239
385PhosphorylationAPEVEDDSLERKRLT
CCCCCCCCHHHHHHH		44.4430108239
392PhosphorylationSLERKRLTRISDPEK
CHHHHHHHCCCCHHH		29.9525159151
395PhosphorylationRKRLTRISDPEKWEI
HHHHHCCCCHHHHHH		43.7725159151
399SumoylationTRISDPEKWEIKQMI
HCCCCHHHHHHHHHH		56.3628112733
399UbiquitinationTRISDPEKWEIKQMI
HCCCCHHHHHHHHHH		56.36-
399SumoylationTRISDPEKWEIKQMI
HCCCCHHHHHHHHHH		56.36-
412PhosphorylationMIAANVLSKEEFPDF
HHHHHCCCCCCCCCC		33.4721406692
456PhosphorylationLRGHTKQSMDMSPIK
CCCCCCCCCCCCCCE		20.5023927012
460PhosphorylationTKQSMDMSPIKIVKN
CCCCCCCCCCEEEEC		21.1429255136
471PhosphorylationIVKNPDGSLSQAAMM
EEECCCCCHHHHHHH		32.0326074081
473PhosphorylationKNPDGSLSQAAMMQS
ECCCCCHHHHHHHHH		21.3326074081
480PhosphorylationSQAAMMQSALAKERR
HHHHHHHHHHHHHHH		13.8326074081
484AcetylationMMQSALAKERRELKQ
HHHHHHHHHHHHHHH		53.2426051181
500PhosphorylationQREAEMDSIPMGLNK
HHHHHHHCCCCCCCH		27.5528555341
539MethylationPNDIPEWKKHAFGGN
CCCCHHHHHHHCCCC		32.78-
547UbiquitinationKHAFGGNKASYGKKT
HHHCCCCCCCCCHHH		41.82-
554PhosphorylationKASYGKKTQMSILEQ
CCCCCHHHHCHHHHH		32.7516094384
556SulfoxidationSYGKKTQMSILEQRE
CCCHHHHCHHHHHHC		3.0521406390
557PhosphorylationYGKKTQMSILEQRES
CCHHHHCHHHHHHCC		17.7616094384
564PhosphorylationSILEQRESLPIYKLK
HHHHHHCCCCHHHHH		41.4529396449
568PhosphorylationQRESLPIYKLKEQLV
HHCCCCHHHHHHHHH		14.3429396449
628UbiquitinationVAAMSVAKRVSEEFG
HHHHHHHHHHHHHHC		51.69-
6282-HydroxyisobutyrylationVAAMSVAKRVSEEFG
HHHHHHHHHHHHHHC		51.69-
645PhosphorylationLGQEVGYTIRFEDCT
CCCCCCEEEEEECCC		10.3524719451
694PhosphorylationAHERTIHTDVLFGLL
HHHHHCHHHHHHHHH		24.77-
702AcetylationDVLFGLLKKTVQKRQ
HHHHHHHHHHHHHHC		51.9826051181
756PhosphorylationTKEPETDYLDASLIT
ECCCCCCCCCHHHEE		17.5726074081
760PhosphorylationETDYLDASLITVMQI
CCCCCCHHHEEEEEE		21.7026074081
763PhosphorylationYLDASLITVMQIHLT
CCCHHHEEEEEEEEC		18.4126074081
868UbiquitinationKQKVYNSKTGIDQLV
CHHHCCCCCCCCEEE		47.32-
885UbiquitinationPISQAQAKQRAGRAG
CCCHHHHHHHCCCCC		28.39-
914PhosphorylationAYRDEMLTTNVPEIQ
HHHHHCHHCCCCHHH		18.2722817900
915PhosphorylationYRDEMLTTNVPEIQR
HHHHCHHCCCCHHHH		30.2022817900
931PhosphorylationNLASTVLSLKAMGIN
CHHHHHHHHHHCCCC		24.4024719451
996PhosphorylationLCKMLIMSVHLGCSE
HHHHHHHHHHCCCCH		10.2121406692
1002PhosphorylationMSVHLGCSEEMLTIV
HHHHCCCCHHHHHHH		34.4921406692
1007PhosphorylationGCSEEMLTIVSMLSV
CCCHHHHHHHHHHCC		20.3021406692
1010PhosphorylationEEMLTIVSMLSVQNV
HHHHHHHHHHCCCCC		15.3421406692
1013PhosphorylationLTIVSMLSVQNVFYR
HHHHHHHCCCCCCCC		17.0221406692
1019PhosphorylationLSVQNVFYRPKDKQA
HCCCCCCCCCCCHHH		23.0221406692
1090UbiquitinationLGIMDRHKLDVVSCG
HCCCCHHCCCEEECC		47.48-
1098UbiquitinationLDVVSCGKSTVRVQK
CCEEECCCCCHHHHH		47.48-
1105UbiquitinationKSTVRVQKAICSGFF
CCCHHHHHHHHCCCC		36.54-
1126PhosphorylationDPQEGYRTLIDQQVV
CCCCCHHHHHCCEEE		21.41-
1202PhosphorylationQQRLEPLYNRYEEPN
HHHHHHHHHHCCCCC		14.33-
1205PhosphorylationLEPLYNRYEEPNAWR
HHHHHHHCCCCCHHH		22.4728796482
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 DHX8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX8_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 DHX8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHF5A_HUMANPHF5Aphysical
22939629
KANL1_HUMANKANSL1physical
22939629
MYPN_HUMANMYPNphysical
22939629
TAF9_HUMANTAF9physical
22939629
RPA2_HUMANPOLR1Bphysical
22939629
PR40A_HUMANPRPF40Aphysical
22365833
CHERP_HUMANCHERPphysical
22365833
PR38A_HUMANPRPF38Aphysical
22365833
ISY1_HUMANISY1physical
22365833
RBMX2_HUMANRBMX2physical
22365833
MFAP1_HUMANMFAP1physical
22365833
DHX8_HUMANDHX8physical
22365833
THOC1_HUMANTHOC1physical
22365833
RBM7_HUMANRBM7physical
22365833
S30BP_HUMANSAP30BPphysical
22365833
NKAP_HUMANNKAPphysical
22365833
ZCH10_HUMANZCCHC10physical
22365833
RL26L_HUMANRPL26L1physical
26186194
RL26_HUMANRPL26physical
26186194
RBM28_HUMANRBM28physical
26186194
SPB1_HUMANFTSJ3physical
26186194
CATIN_HUMANCACTINphysical
26186194
SRPK1_HUMANSRPK1physical
26186194
SRPK2_HUMANSRPK2physical
26186194
RL10A_HUMANRPL10Aphysical
26186194
RL5_HUMANRPL5physical
26186194
CK057_HUMANC11orf57physical
26186194
SYF1_HUMANXAB2physical
26186194
RL1D1_HUMANRSL1D1physical
26186194
CRNL1_HUMANCRNKL1physical
26186194
CDC5L_HUMANCDC5Lphysical
26186194
AQR_HUMANAQRphysical
26186194
NUDC1_HUMANNUDCD1physical
26186194
SNW1_HUMANSNW1physical
26186194
RBMX2_HUMANRBMX2physical
26186194
MORC2_HUMANMORC2physical
26186194
SAHH3_HUMANAHCYL2physical
26186194
SAHH2_HUMANAHCYL1physical
26186194
ISY1_HUMANISY1physical
26186194
NOP2_HUMANNOP2physical
26186194
CCD12_HUMANCCDC12physical
26186194
RL15_HUMANRPL15physical
26186194
JMJD6_HUMANJMJD6physical
26186194
RL32_HUMANRPL32physical
26186194
RL36L_HUMANRPL36ALphysical
26186194
PRP17_HUMANCDC40physical
26186194
CK057_HUMANC11orf57physical
28514442
JMJD6_HUMANJMJD6physical
28514442
NUDC1_HUMANNUDCD1physical
28514442
CATIN_HUMANCACTINphysical
28514442
SAHH3_HUMANAHCYL2physical
28514442
CRNL1_HUMANCRNKL1physical
28514442
RL26L_HUMANRPL26L1physical
28514442
SRPK1_HUMANSRPK1physical
28514442
SAHH2_HUMANAHCYL1physical
28514442
ISY1_HUMANISY1physical
28514442
AQR_HUMANAQRphysical
28514442
MORC2_HUMANMORC2physical
28514442
SYF1_HUMANXAB2physical
28514442
RL36L_HUMANRPL36ALphysical
28514442
PRP17_HUMANCDC40physical
28514442
SNW1_HUMANSNW1physical
28514442
SYF2_HUMANSYF2physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
PPIE_HUMANPPIEphysical
28514442
CCD12_HUMANCCDC12physical
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 DHX8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-395, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-228 ANDSER-230, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-554 AND SER-557, ANDMASS SPECTROMETRY.

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