DDX55_HUMAN - dbPTM
DDX55_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX55_HUMAN
UniProt AC Q8NHQ9
Protein Name ATP-dependent RNA helicase DDX55
Gene Name DDX55
Organism Homo sapiens (Human).
Sequence Length 600
Subcellular Localization
Protein Description Probable ATP-binding RNA helicase..
Protein Sequence MEHVTEGSWESLPVPLHPQVLGALRELGFPYMTPVQSATIPLFMRNKDVAAEAVTGSGKTLAFVIPILEILLRREEKLKKSQVGAIIITPTRELAIQIDEVLSHFTKHFPEFSQILWIGGRNPGEDVERFKQQGGNIIVATPGRLEDMFRRKAEGLDLASCVRSLDVLVLDEADRLLDMGFEASINTILEFLPKQRRTGLFSATQTQEVENLVRAGLRNPVRVSVKEKGVAASSAQKTPSRLENYYMVCKADEKFNQLVHFLRNHKQEKHLVFFSTCACVEYYGKALEVLVKGVKIMCIHGKMKYKRNKIFMEFRKLQSGILVCTDVMARGIDIPEVNWVLQYDPPSNASAFVHRCGRTARIGHGGSALVFLLPMEESYINFLAINQKCPLQEMKPQRNTADLLPKLKSMALADRAVFEKGMKAFVSYVQAYAKHECNLIFRLKDLDFASLARGFALLRMPKMPELRGKQFPDFVPVDVNTDTIPFKDKIREKQRQKLLEQQRREKTENEGRRKFIKNKAWSKQKAKKEKKKKMNEKRKREEGSDIEDEDMEELLNDTRLLKKLKKGKITEEEFEKGLLTTGKRTIKTVDLGISDLEDDC
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
31PhosphorylationLRELGFPYMTPVQSA
HHHHCCCCCCCCCCC		16.0321406692
33PhosphorylationELGFPYMTPVQSATI
HHCCCCCCCCCCCCC		17.9221406692
37PhosphorylationPYMTPVQSATIPLFM
CCCCCCCCCCCCEEE		27.8421406692
39PhosphorylationMTPVQSATIPLFMRN
CCCCCCCCCCEEECC		28.5121406692
47UbiquitinationIPLFMRNKDVAAEAV
CCEEECCCCHHHHHH		43.12-
47AcetylationIPLFMRNKDVAAEAV
CCEEECCCCHHHHHH		43.1226051181
55PhosphorylationDVAAEAVTGSGKTLA
CHHHHHHCCCCHHHH		32.4521406692
57PhosphorylationAAEAVTGSGKTLAFV
HHHHHCCCCHHHHHH		27.9621406692
81PhosphorylationREEKLKKSQVGAIII
CHHHHHHCCCCCEEE		28.6321406692
89PhosphorylationQVGAIIITPTRELAI
CCCCEEECCCHHHHH		14.2724719451
91PhosphorylationGAIIITPTRELAIQI
CCEEECCCHHHHHHH		28.2921406692
141PhosphorylationGGNIIVATPGRLEDM
CCCEEEECCCCHHHH		18.5125159151
1522-HydroxyisobutyrylationLEDMFRRKAEGLDLA
HHHHHHHHCCCCCHH		46.67-
152UbiquitinationLEDMFRRKAEGLDLA
HHHHHHHHCCCCCHH		46.67-
218MethylationNLVRAGLRNPVRVSV
HHHHCCCCCCEEEEH		44.48-
224PhosphorylationLRNPVRVSVKEKGVA
CCCCEEEEHHHCCCC		19.5329449344
228AcetylationVRVSVKEKGVAASSA
EEEEHHHCCCCCCCC		53.6325953088
233PhosphorylationKEKGVAASSAQKTPS
HHCCCCCCCCCCCCH		19.2327251789
234PhosphorylationEKGVAASSAQKTPSR
HCCCCCCCCCCCCHH		29.9618220336
237AcetylationVAASSAQKTPSRLEN
CCCCCCCCCCHHHHH		63.2225953088
237UbiquitinationVAASSAQKTPSRLEN
CCCCCCCCCCHHHHH		63.22-
238PhosphorylationAASSAQKTPSRLENY
CCCCCCCCCHHHHHE		17.8925159151
254AcetylationMVCKADEKFNQLVHF
EEEEHHHHHHHHHHH		50.6026051181
305PhosphorylationCIHGKMKYKRNKIFM
EECCCCCCCCCCHHH		16.2222817900
316UbiquitinationKIFMEFRKLQSGILV
CHHHHHHHHHCCEEE		57.0821906983
319PhosphorylationMEFRKLQSGILVCTD
HHHHHHHCCEEEEEC		37.9323532336
406AcetylationNTADLLPKLKSMALA
CHHHHHHHHHHHHHH		69.3926051181
409PhosphorylationDLLPKLKSMALADRA
HHHHHHHHHHHHHHH		21.5230576142
427PhosphorylationKGMKAFVSYVQAYAK
HHHHHHHHHHHHHHH		17.0923401153
444AcetylationCNLIFRLKDLDFASL
CCEEEEECCCCHHHH		52.5719608861
469UbiquitinationKMPELRGKQFPDFVP
CCHHHCCCCCCCCCC		42.19-
517AcetylationEGRRKFIKNKAWSKQ
HHHHHHHHHHHHHHH		56.3790733
519AcetylationRRKFIKNKAWSKQKA
HHHHHHHHHHHHHHH		46.3590735
522O-linked_GlycosylationFIKNKAWSKQKAKKE
HHHHHHHHHHHHHHH		30.0328510447
523AcetylationIKNKAWSKQKAKKEK
HHHHHHHHHHHHHHH		45.1590737
544PhosphorylationKRKREEGSDIEDEDM
HHHHHCCCCCCHHHH		38.4029255136
558PhosphorylationMEELLNDTRLLKKLK
HHHHHHHHHHHHHHH		23.3423927012
583AcetylationKGLLTTGKRTIKTVD
HCCCCCCCCEEEEEE		44.2525953088
5832-HydroxyisobutyrylationKGLLTTGKRTIKTVD
HCCCCCCCCEEEEEE		44.25-
585PhosphorylationLLTTGKRTIKTVDLG
CCCCCCCEEEEEECC		30.2528111955
588PhosphorylationTGKRTIKTVDLGISD
CCCCEEEEEECCCHH		18.5326552605
594PhosphorylationKTVDLGISDLEDDC-
EEEECCCHHCCCCC-		34.0525159151
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 DDX55_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX55_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 DDX55_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KR108_HUMANKRTAP10-8physical
25416956
DDX56_HUMANDDX56physical
26344197
RL23_HUMANRPL23physical
26344197
SETD4_HUMANSETD4physical
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 DDX55_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND MASS SPECTROMETRY.
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-544, 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-544, AND MASSSPECTROMETRY.
"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 SER-544, AND MASSSPECTROMETRY.

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