DDX56_HUMAN - dbPTM
DDX56_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX56_HUMAN
UniProt AC Q9NY93
Protein Name Probable ATP-dependent RNA helicase DDX56
Gene Name DDX56
Organism Homo sapiens (Human).
Sequence Length 547
Subcellular Localization Nucleus, nucleolus .
Protein Description May play a role in later stages of the processing of the pre-ribosomal particles leading to mature 60S ribosomal subunits. Has intrinsic ATPase activity..
Protein Sequence MEDSEALGFEHMGLDPRLLQAVTDLGWSRPTLIQEKAIPLALEGKDLLARARTGSGKTAAYAIPMLQLLLHRKATGPVVEQAVRGLVLVPTKELARQAQSMIQQLATYCARDVRVANVSAAEDSVSQRAVLMEKPDVVVGTPSRILSHLQQDSLKLRDSLELLVVDEADLLFSFGFEEELKSLLCHLPRIYQAFLMSATFNEDVQALKELILHNPVTLKLQESQLPGPDQLQQFQVVCETEEDKFLLLYALLKLSLIRGKSLLFVNTLERSYRLRLFLEQFSIPTCVLNGELPLRSRCHIISQFNQGFYDCVIATDAEVLGAPVKGKRRGRGPKGDKASDPEAGVARGIDFHHVSAVLNFDLPPTPEAYIHRAGRTARANNPGIVLTFVLPTEQFHLGKIEELLSGENRGPILLPYQFRMEEIEGFRYRCRDAMRSVTKQAIREARLKEIKEELLHSEKLKTYFEDNPRDLQLLRHDLPLHPAVVKPHLGHVPDYLVPPALRGLVRPHKKRKKLSSSCRKAKRAKSQNPLRSFKHKGKKFRPTAKPS
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
1Acetylation-------MEDSEALG
-------CCHHHHHC		13.41-
28PhosphorylationAVTDLGWSRPTLIQE
HHHHCCCCCCHHHHH		26.9524719451
362-HydroxyisobutyrylationRPTLIQEKAIPLALE
CCHHHHHCCCCHHHC		34.93-
36UbiquitinationRPTLIQEKAIPLALE
CCHHHHHCCCCHHHC		34.9329967540
452-HydroxyisobutyrylationIPLALEGKDLLARAR
CCHHHCCHHHHHHCC		35.51-
45UbiquitinationIPLALEGKDLLARAR
CCHHHCCHHHHHHCC		35.5127667366
73UbiquitinationLQLLLHRKATGPVVE
HHHHHHHHCCCHHHH		39.2824816145
91PhosphorylationRGLVLVPTKELARQA
HCCEEEEHHHHHHHH		29.6720068231
92UbiquitinationGLVLVPTKELARQAQ
CCEEEEHHHHHHHHH		44.6633845483
108PhosphorylationMIQQLATYCARDVRV
HHHHHHHHHHHCCHH		4.40-
119PhosphorylationDVRVANVSAAEDSVS
CCHHHCCCCCCCCHH		22.90-
124PhosphorylationNVSAAEDSVSQRAVL
CCCCCCCCHHHHCHH		18.3819691289
126PhosphorylationSAAEDSVSQRAVLME
CCCCCCHHHHCHHHC		20.2117525332
134UbiquitinationQRAVLMEKPDVVVGT
HHCHHHCCCCEEEEC		32.3321906983
134AcetylationQRAVLMEKPDVVVGT
HHCHHHCCCCEEEEC		32.3326051181
141PhosphorylationKPDVVVGTPSRILSH
CCCEEEECHHHHHHH		13.3825159151
143PhosphorylationDVVVGTPSRILSHLQ
CEEEECHHHHHHHHH		31.6120860994
155UbiquitinationHLQQDSLKLRDSLEL
HHHHHCCHHHHCCEE		45.4922817900
219UbiquitinationLHNPVTLKLQESQLP
HCCCCEEEECHHCCC		38.4729967540
285PhosphorylationLEQFSIPTCVLNGEL
HHHHCCCCCEECCCC		17.36-
296PhosphorylationNGELPLRSRCHIISQ
CCCCCCHHCEEHHHH		47.12-
337UbiquitinationGRGPKGDKASDPEAG
CCCCCCCCCCCCCCH		59.4633845483
339PhosphorylationGPKGDKASDPEAGVA
CCCCCCCCCCCCHHC		60.4819691289
399UbiquitinationTEQFHLGKIEELLSG
HHHEEHHHHHHHHCC		53.9929967540
408UbiquitinationEELLSGENRGPILLP
HHHHCCCCCCCEEEE		58.7029967540
411UbiquitinationLSGENRGPILLPYQF
HCCCCCCCEEEEEEE		15.7129967540
419UbiquitinationILLPYQFRMEEIEGF
EEEEEEEEHHHHHCH		18.9733845483
420SulfoxidationLLPYQFRMEEIEGFR
EEEEEEEHHHHHCHH		5.9821406390
421UbiquitinationLPYQFRMEEIEGFRY
EEEEEEHHHHHCHHH		52.1233845483
439UbiquitinationDAMRSVTKQAIREAR
HHHHHHHHHHHHHHH		35.2629967540
446UbiquitinationKQAIREARLKEIKEE
HHHHHHHHHHHHHHH		41.3533845483
448UbiquitinationAIREARLKEIKEELL
HHHHHHHHHHHHHHH		52.4129967540
451SumoylationEARLKEIKEELLHSE
HHHHHHHHHHHHCCH		46.34-
451AcetylationEARLKEIKEELLHSE
HHHHHHHHHHHHCCH		46.3426051181
451SumoylationEARLKEIKEELLHSE
HHHHHHHHHHHHCCH		46.34-
451UbiquitinationEARLKEIKEELLHSE
HHHHHHHHHHHHCCH		46.3429967540
459UbiquitinationEELLHSEKLKTYFED
HHHHCCHHHHHHHCC		59.2933845483
461UbiquitinationLLHSEKLKTYFEDNP
HHCCHHHHHHHCCCH		52.8533845483
462PhosphorylationLHSEKLKTYFEDNPR
HCCHHHHHHHCCCHH		43.8322210691
463PhosphorylationHSEKLKTYFEDNPRD
CCHHHHHHHCCCHHH		11.9022210691
485UbiquitinationLPLHPAVVKPHLGHV
CCCCHHHCCCCCCCC		9.6729967540
486AcetylationPLHPAVVKPHLGHVP
CCCHHHCCCCCCCCC		21.8126051181
486UbiquitinationPLHPAVVKPHLGHVP
CCCHHHCCCCCCCCC		21.8133845483
495PhosphorylationHLGHVPDYLVPPALR
CCCCCCCCCCCHHHH		11.9727642862
525UbiquitinationCRKAKRAKSQNPLRS
HHHHHHHHHCCCCHH		57.5229967540
526PhosphorylationRKAKRAKSQNPLRSF
HHHHHHHHCCCCHHC		33.9224850871
532PhosphorylationKSQNPLRSFKHKGKK
HHCCCCHHCCCCCCC		46.4525159151
547PhosphorylationFRPTAKPS-------
CCCCCCCC-------		52.7425159151
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 DDX56_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX56_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 DDX56_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBB1A_HUMANMYBBP1Aphysical
17353931
RT25_HUMANMRPS25physical
17353931
RS3A_HUMANRPS3Aphysical
17353931
RRP12_HUMANRRP12physical
17353931
RL34_HUMANRPL34physical
17353931
RS9_HUMANRPS9physical
17353931
RL18A_HUMANRPL18Aphysical
17353931
RL23A_HUMANRPL23Aphysical
17353931
RT05_HUMANMRPS5physical
17353931
RL26_HUMANRPL26physical
17353931
RS16_HUMANRPS16physical
17353931
SPB1_HUMANFTSJ3physical
17353931
NOG2_HUMANGNL2physical
17353931
RT24_HUMANMRPS24physical
17353931
RT14_HUMANMRPS14physical
17353931
DHX57_HUMANDHX57physical
17353931
RL31_HUMANRPL31physical
17353931
RL37_HUMANRPL37physical
17353931
RT09_HUMANMRPS9physical
17353931
FBRL_HUMANFBLphysical
17353931
RS29_HUMANRPS29physical
17353931
RS11_HUMANRPS11physical
17353931
RL29_HUMANRPL29physical
17353931
RM43_HUMANMRPL43physical
17353931
SRP14_HUMANSRP14physical
17353931
RT34_HUMANMRPS34physical
17353931
DHX37_HUMANDHX37physical
17353931
UBP33_HUMANUSP33physical
16169070
SOX30_HUMANSOX30physical
21988832
EHD2_HUMANEHD2physical
21988832
AATF_HUMANAATFphysical
26344197
CEBPZ_HUMANCEBPZphysical
26344197
DDX10_HUMANDDX10physical
26344197
GRWD1_HUMANGRWD1physical
26344197
PUM3_HUMANKIAA0020physical
26344197
MRT4_HUMANMRTO4physical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOLC1_HUMANNOLC1physical
26344197
NOP2_HUMANNOP2physical
26344197
RPF2_HUMANRPF2physical
26344197
RL5_HUMANRPL5physical
26344197
RRS1_HUMANRRS1physical
26344197
TBL3_HUMANTBL3physical
26344197
U2AF1_HUMANU2AF1physical
26344197
UT14A_HUMANUTP14Aphysical
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 DDX56_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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-126, AND MASSSPECTROMETRY.

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