DDX51_HUMAN - dbPTM
DDX51_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX51_HUMAN
UniProt AC Q8N8A6
Protein Name ATP-dependent RNA helicase DDX51
Gene Name DDX51
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Nucleus, nucleolus.
Protein Description ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits..
Protein Sequence MALFYVARYPGPDAAAAAGPEGAEAGAHGRARALLERLQSRARERQQQREPAQTEAAASTEPATRRRRRPRRRRRVNDAEPGSPEAPQGKRRKADGEDAGAESNEEAPGEPSAGSSEEAPGEPSAGSSEEAPGERSTSASAEAAPDGPALEEAAGPLVPGLVLGGFGKRKAPKVQPFLPRWLAEPNCVRRNVTEDLVPIEDIPDVHPDLQKQLRAHGISSYFPVQAAVIPALLESAACGFLVGRGGYRPSDLCVSAPTGSGKTLAFVIPVVQALLSRVVCHIRALVVLPTKELAQQVSKVFNIYTDATPLRVSLVTGQKSLAKEQESLVQKTADGYRCLADIVVATPGRLVDHIDQTPGFSLQQLRFLIIDEADRMIDSMHQSWLPRVVAAAFQSEDPADPCALLQRRQAQAVTAASTCCPQMPLQKLLFSATLTQNPEKLQQLGLHQPRLFSTGLAHRGLEDTDGDGDSGKYAFPVGLTHHYVPCSLSSKPLVVLHLVLEMGFSRVLCFTNSRENSHRLFLLVQAFGGVDVAEFSSRYGPGQRRMILKQFEQGKIQLLISTDATARGIDVQGVELVVNYDAPQYLRTYVHRVGRTARAGKTGQAFTLLLKVQERRFLRMLTEAGAPELQRHELSSKLLQPLVPRYEEALSQLEESVKEERKQRAA
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------MALFYVARY
------CCEEEEECC		13.3322223895
8MethylationMALFYVARYPGPDAA
CCEEEEECCCCCHHH		28.30-
30MethylationAEAGAHGRARALLER
HHCCHHHHHHHHHHH		15.84-
59PhosphorylationAQTEAAASTEPATRR
HHHHHHHCCCHHHHH		28.6920860994
60PhosphorylationQTEAAASTEPATRRR
HHHHHHCCCHHHHHH		41.0620860994
64PhosphorylationAASTEPATRRRRRPR
HHCCCHHHHHHCCCC		35.1128555341
83PhosphorylationVNDAEPGSPEAPQGK
CCCCCCCCCCCCCCC		30.2219664994
90AcetylationSPEAPQGKRRKADGE
CCCCCCCCCCCCCCC		43.7225953088
103PhosphorylationGEDAGAESNEEAPGE
CCCCCCCCCCCCCCC		49.3528355574
112PhosphorylationEEAPGEPSAGSSEEA
CCCCCCCCCCCCCCC		40.7428176443
115PhosphorylationPGEPSAGSSEEAPGE
CCCCCCCCCCCCCCC		34.0030278072
116PhosphorylationGEPSAGSSEEAPGEP
CCCCCCCCCCCCCCC		38.2430278072
124PhosphorylationEEAPGEPSAGSSEEA
CCCCCCCCCCCCCCC		40.7423663014
127PhosphorylationPGEPSAGSSEEAPGE
CCCCCCCCCCCCCCC		34.0023663014
128PhosphorylationGEPSAGSSEEAPGER
CCCCCCCCCCCCCCC		38.2423663014
138PhosphorylationAPGERSTSASAEAAP
CCCCCCCCCCCCCCC		22.82-
211UbiquitinationDVHPDLQKQLRAHGI
CCCHHHHHHHHHCCC		59.6122817900
235PhosphorylationVIPALLESAACGFLV
HHHHHHHHHHCCCEE		22.5724719451
247PhosphorylationFLVGRGGYRPSDLCV
CEECCCCCCHHHEEE		23.3620068231
250PhosphorylationGRGGYRPSDLCVSAP
CCCCCCHHHEEEECC		33.9320068231
255PhosphorylationRPSDLCVSAPTGSGK
CHHHEEEECCCCCCC		27.7720068231
258PhosphorylationDLCVSAPTGSGKTLA
HEEEECCCCCCCHHH		43.6320068231
260PhosphorylationCVSAPTGSGKTLAFV
EEECCCCCCCHHHHH		39.3320068231
291UbiquitinationALVVLPTKELAQQVS
EEEEECHHHHHHHHH		49.11-
299UbiquitinationELAQQVSKVFNIYTD
HHHHHHHHHHCCCCC		52.57-
304PhosphorylationVSKVFNIYTDATPLR
HHHHHCCCCCCCCCE		10.3222817900
319UbiquitinationVSLVTGQKSLAKEQE
EEEHHCCHHHHHHHH		49.1029967540
323UbiquitinationTGQKSLAKEQESLVQ
HCCHHHHHHHHHHHH		66.2829967540
331UbiquitinationEQESLVQKTADGYRC
HHHHHHHHHCCHHHH		37.90-
331AcetylationEQESLVQKTADGYRC
HHHHHHHHHCCHHHH		37.9026051181
346PhosphorylationLADIVVATPGRLVDH
HEEEEEECCCCCCCC		18.0528674419
402GlutathionylationSEDPADPCALLQRRQ
CCCCCCHHHHHHHHH		4.2522555962
431PhosphorylationPLQKLLFSATLTQNP
HHHHHHHHHHHCCCH		21.9520068231
433PhosphorylationQKLLFSATLTQNPEK
HHHHHHHHHCCCHHH		29.1920068231
435PhosphorylationLLFSATLTQNPEKLQ
HHHHHHHCCCHHHHH		23.1919664994
440UbiquitinationTLTQNPEKLQQLGLH
HHCCCHHHHHHCCCC		53.5029967540
464PhosphorylationAHRGLEDTDGDGDSG
CCCCCCCCCCCCCCC		32.2928674419
470PhosphorylationDTDGDGDSGKYAFPV
CCCCCCCCCCEEEEE		42.5928985074
490PhosphorylationYVPCSLSSKPLVVLH
EECCCCCCCCCHHHH		43.5224719451
561PhosphorylationGKIQLLISTDATARG
CCEEEEEECCCCCCC		21.8720068231
562PhosphorylationKIQLLISTDATARGI
CEEEEEECCCCCCCC		23.7420068231
565PhosphorylationLLISTDATARGIDVQ
EEEECCCCCCCCCCC		21.5020068231
585PhosphorylationVNYDAPQYLRTYVHR
EECCHHHHHHHHHHH		9.33-
588PhosphorylationDAPQYLRTYVHRVGR
CHHHHHHHHHHHHCC		27.57-
596PhosphorylationYVHRVGRTARAGKTG
HHHHHCCCCCCCCCC		17.9924719451
601AcetylationGRTARAGKTGQAFTL
CCCCCCCCCCHHHHH		48.8025953088
601UbiquitinationGRTARAGKTGQAFTL
CCCCCCCCCCHHHHH		48.80-
607PhosphorylationGKTGQAFTLLLKVQE
CCCCHHHHHHHHHHH		21.3628674151
620SulfoxidationQERRFLRMLTEAGAP
HHHHHHHHHHHCCCH		6.2121406390
635PhosphorylationELQRHELSSKLLQPL
HHHHHHHHHHHHHHH		23.5727174698
636PhosphorylationLQRHELSSKLLQPLV
HHHHHHHHHHHHHHH		39.6927174698
637UbiquitinationQRHELSSKLLQPLVP
HHHHHHHHHHHHHHH		50.2522505724
658AcetylationSQLEESVKEERKQRA
HHHHHHHHHHHHHHH		64.2426051181
658UbiquitinationSQLEESVKEERKQRA
HHHHHHHHHHHHHHH		64.2429967540
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 DDX51_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX51_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 DDX51_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DDX51_HUMAN !!
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 DDX51_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-83, 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-83, 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-83 AND SER-103, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"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-83 AND SER-103, 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-83, AND MASSSPECTROMETRY.
"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-83, AND MASSSPECTROMETRY.

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