dbPTM

DDX47_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX47_HUMAN
UniProt AC	Q9H0S4
Protein Name	Probable ATP-dependent RNA helicase DDX47
Gene Name	DDX47
Organism	Homo sapiens (Human).
Sequence Length	455
Subcellular Localization	Nucleus, nucleolus . Localizes in the nucleolar-organizing region during ribosome biogenesis.
Protein Description	Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors..
Protein Sequence	MAAPEEHDSPTEASQPIVEEEETKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPGFPTQDDEVMMLTERVAEAQRFARMELREHGEKKKRSREDAGDNDDTEGAIGVRNKVAGGKMKKRKGR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAPEEHDS ------CCCCCCCCC	31.55	21406692
9	Phosphorylation	AAPEEHDSPTEASQP CCCCCCCCCCCCCCC	35.31	29255136
11	Phosphorylation	PEEHDSPTEASQPIV CCCCCCCCCCCCCCC	48.40	29255136
14	Phosphorylation	HDSPTEASQPIVEEE CCCCCCCCCCCCCHH	30.20	29255136
23	Phosphorylation	PIVEEEETKTFKDLG CCCCHHHHCCHHHCC	38.37	23663014
24	Sumoylation	IVEEEETKTFKDLGV CCCHHHHCCHHHCCC	56.07	-
46	Ubiquitination	CDQLGWTKPTKIQIE HHHHCCCCCCEEEEE	44.15	-
46	Acetylation	CDQLGWTKPTKIQIE HHHHCCCCCCEEEEE	44.15	26051181
49	Ubiquitination	LGWTKPTKIQIEAIP HCCCCCCEEEEEEEC	40.93	-
74	Ubiquitination	LAETGSGKTGAFALP EEECCCCHHHHCHHH	45.54	-
99	Phosphorylation	RLFALVLTPTRELAF HHHHHHHCCCHHHHH	18.35	24719451
142	Acetylation	QSLALAKKPHIIIAT HHHHHCCCCEEEEEC	35.90	26051181
142	Ubiquitination	QSLALAKKPHIIIAT HHHHHCCCCEEEEEC	35.90	-
149	Phosphorylation	KPHIIIATPGRLIDH CCEEEEECCCCHHHH	18.83	28985074
161	Ubiquitination	IDHLENTKGFNLRAL HHHHHHCCCCCHHHH	73.43	21890473
161	2-Hydroxyisobutyrylation	IDHLENTKGFNLRAL HHHHHHCCCCCHHHH	73.43	-
161	Ubiquitination	IDHLENTKGFNLRAL HHHHHHCCCCCHHHH	73.43	21890473
161	Acetylation	IDHLENTKGFNLRAL HHHHHHCCCCCHHHH	73.43	26051181
169	2-Hydroxyisobutyrylation	GFNLRALKYLVMDEA CCCHHHHHHHHCCHH	35.24	-
169	Acetylation	GFNLRALKYLVMDEA CCCHHHHHHHHCCHH	35.24	26051181
169	Ubiquitination	GFNLRALKYLVMDEA CCCHHHHHHHHCCHH	35.24	2190698
182	Sulfoxidation	EADRILNMDFETEVD HHHHHHCCCCHHHHH	5.83	21406390
186	Phosphorylation	ILNMDFETEVDKILK HHCCCCHHHHHHHHH	41.10	-
190	Ubiquitination	DFETEVDKILKVIPR CCHHHHHHHHHHCCC	55.93	-
193	Ubiquitination	TEVDKILKVIPRDRK HHHHHHHHHCCCCCC	41.41	-
201	Phosphorylation	VIPRDRKTFLFSATM HCCCCCCEEEEEEHH	26.85	-
221	Ubiquitination	KLQRAALKNPVKCAV HHHHHHHHCHHHHHH	55.25	-
225	Ubiquitination	AALKNPVKCAVSSKY HHHHCHHHHHHCCCC	20.10	-
231	Acetylation	VKCAVSSKYQTVEKL HHHHHCCCCCHHHHH	33.59	25953088
231	Ubiquitination	VKCAVSSKYQTVEKL HHHHHCCCCCHHHHH	33.59	-
247	Phosphorylation	QYYIFIPSKFKDTYL HEEEECCHHCCCEEH	46.00	24719451
279	Phosphorylation	TCNNTQRTALLLRNL CCCCHHHHHHHHHHH	16.31	20068231
289	Phosphorylation	LLRNLGFTAIPLHGQ HHHHHCCCEEECCCC	23.14	20068231
301	Ubiquitination	HGQMSQSKRLGSLNK CCCCCCCCCCCCHHH	43.96	-
308	Acetylation	KRLGSLNKFKAKARS CCCCCHHHHHHHHHH	54.24	25953088
308	Ubiquitination	KRLGSLNKFKAKARS CCCCCHHHHHHHHHH	54.24	-
310	Acetylation	LGSLNKFKAKARSIL CCCHHHHHHHHHHHH	51.06	11790027
312	Acetylation	SLNKFKAKARSILLA CHHHHHHHHHHHHHH	44.94	11790037
315	Phosphorylation	KFKAKARSILLATDV HHHHHHHHHHHHHHH	23.58	22817900
320	Phosphorylation	ARSILLATDVASRGL HHHHHHHHHHHHCCC	30.86	-
354	Phosphorylation	YIHRVGRTARAGRSG HHHHHHCCCCCCCCC	17.99	22210691
362	Ubiquitination	ARAGRSGKAITFVTQ CCCCCCCCEEEEEEE	37.55	-
365	Phosphorylation	GRSGKAITFVTQYDV CCCCCEEEEEEEHHH	19.53	22210691
385	Ubiquitination	IEHLIGKKLPGFPTQ HHHHHCCCCCCCCCC	55.49	-
424	Phosphorylation	HGEKKKRSREDAGDN HHHHHCCCHHCCCCC	49.23	18669648
434	Phosphorylation	DAGDNDDTEGAIGVR CCCCCCCCCCHHHHH	38.90	21815630
443	Acetylation	GAIGVRNKVAGGKMK CHHHHHCCCCCCCCC	23.93	7481495
448	Acetylation	RNKVAGGKMKKRKGR HCCCCCCCCCCCCCC	46.78	90983
451	Acetylation	VAGGKMKKRKGR--- CCCCCCCCCCCC---	56.71	90987

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 DDX47_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DDX47_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 DDX47_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
EXOS4_HUMAN	EXOSC4	physical	22939629
RASK_HUMAN	KRAS	physical	21988832
CDC5L_HUMAN	CDC5L	physical	26344197
DCA13_HUMAN	DCAF13	physical	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 DDX47_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-424, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-9 AND SER-14, AND MASSSPECTROMETRY.	19007248 [Abstract]