dbPTM

DDX52_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX52_HUMAN
UniProt AC	Q9Y2R4
Protein Name	Probable ATP-dependent RNA helicase DDX52
Gene Name	DDX52
Organism	Homo sapiens (Human).
Sequence Length	599
Subcellular Localization	Nucleus, nucleolus .
Protein Description
Protein Sequence	MDVHDLFRRLGAGAKFDTRRFSADAARFQIGKRKYDFDSSEVLQGLDFFGNKKSVPGVCGASQTHQKPQNGEKKEESLTERKREQSKKKRKTMTSEIASQEEGATIQWMSSVEAKIEDKKVQRESKLTSGKLENLRKEKINFLRNKHKIHVQGTDLPDPIATFQQLDQEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDLASVEWLVVDESDKLFEDGKTGFRDQLASIFLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELLFVGSETGKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQAGCPVPEYIKGFQKLLSKQKKKMIKKPLERESISTTPKCFLEKAKDKQKKVTGQNSKKKVALEDKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Acetylation	RRLGAGAKFDTRRFS HHHCCCCCCCCCCCC	42.74	19608861
22	Phosphorylation	KFDTRRFSADAARFQ CCCCCCCCCCHHHHC	24.35	23401153
27	Methylation	RFSADAARFQIGKRK CCCCCHHHHCCCCCC	26.23	-
34	Acetylation	RFQIGKRKYDFDSSE HHCCCCCCCCCCHHH	53.29	26051181
35	Phosphorylation	FQIGKRKYDFDSSEV HCCCCCCCCCCHHHH	26.35	18669648
39	Phosphorylation	KRKYDFDSSEVLQGL CCCCCCCHHHHHHCC	28.52	18669648
40	Phosphorylation	RKYDFDSSEVLQGLD CCCCCCHHHHHHCCC	33.30	21712546
52	Ubiquitination	GLDFFGNKKSVPGVC CCCCCCCCCCCCCCC	46.97	-
52	Acetylation	GLDFFGNKKSVPGVC CCCCCCCCCCCCCCC	46.97	26051181
53	Ubiquitination	LDFFGNKKSVPGVCG CCCCCCCCCCCCCCC	61.76	-
77	Phosphorylation	NGEKKEESLTERKRE CCCCHHHHHHHHHHH	41.50	22468782
92	Phosphorylation	QSKKKRKTMTSEIAS HHHHHHHHHHHHHHH	29.70	22468782
94	Phosphorylation	KKKRKTMTSEIASQE HHHHHHHHHHHHHHC	28.56	30576142
99	Phosphorylation	TMTSEIASQEEGATI HHHHHHHHHCCCCCE	43.73	17525332
105	Phosphorylation	ASQEEGATIQWMSSV HHHCCCCCEEEHHHH	25.26	27251275
110	Phosphorylation	GATIQWMSSVEAKIE CCCEEEHHHHHHHHC	28.42	30576142
111	Phosphorylation	ATIQWMSSVEAKIED CCEEEHHHHHHHHCC	14.10	-
131	Acetylation	ESKLTSGKLENLRKE HHCCCCCHHHHHHHH	53.01	23749302
131	Ubiquitination	ESKLTSGKLENLRKE HHCCCCCHHHHHHHH	53.01	-
139	Ubiquitination	LENLRKEKINFLRNK HHHHHHHHHHHHHCC	46.08	-
148	Ubiquitination	NFLRNKHKIHVQGTD HHHHCCCCEECCCCC	35.80	-
171	Ubiquitination	QQLDQEYKINSRLLQ HHHCHHHHHCHHHHH	34.36	-
228	Ubiquitination	IPILMQLKQPANKGF HHHHHHCCCCCCCCC	37.03	-
258	Phosphorylation	HRELIKISEGTGFRI HHHHHHHHCCCCCEE	25.60	20068231
261	Phosphorylation	LIKISEGTGFRIHMI HHHHHCCCCCEEEEH	29.15	20068231
270	Ubiquitination	FRIHMIHKAAVAAKK CEEEEHHHHHHHHHH	27.41	-
282	Phosphorylation	AKKFGPKSSKKFDIL HHHHCCCCCCCCEEE	50.99	29759185
283	Phosphorylation	KKFGPKSSKKFDILV HHHCCCCCCCCEEEE	46.09	29759185
285	2-Hydroxyisobutyrylation	FGPKSSKKFDILVTT HCCCCCCCCEEEEEC	50.66	-
291	Phosphorylation	KKFDILVTTPNRLIY CCCEEEEECCCCEEE	32.84	23312004
292	Phosphorylation	KFDILVTTPNRLIYL CCEEEEECCCCEEEE	15.87	23312004
328	Ubiquitination	DKLFEDGKTGFRDQL HHHCCCCCCCHHHHH	58.77	-
328	2-Hydroxyisobutyrylation	DKLFEDGKTGFRDQL HHHCCCCCCCHHHHH	58.77	-
409	Ubiquitination	AMRELVKKGFNPPVL HHHHHHHCCCCCCEE	62.34	-
454	Phosphorylation	TQQQRDNTVHSFRAG HHHHHCCCCHHHHHH	24.72	20873877
457	Phosphorylation	QRDNTVHSFRAGKIW HHCCCCHHHHHHHHH	16.46	20873877
511	Ubiquitination	GRAGNKGKAITFFTE CCCCCCCCEEEEECC	37.92	-
521	Ubiquitination	TFFTEDDKPLLRSVA EEECCCCHHHHHHHH	50.30	-
521	Acetylation	TFFTEDDKPLLRSVA EEECCCCHHHHHHHH	50.30	26051181
536	Glutathionylation	NVIQQAGCPVPEYIK HHHHHCCCCHHHHHH	3.26	22555962
543	Acetylation	CPVPEYIKGFQKLLS CCHHHHHHHHHHHHH	53.42	26051181
543	Ubiquitination	CPVPEYIKGFQKLLS CCHHHHHHHHHHHHH	53.42	-
547	Ubiquitination	EYIKGFQKLLSKQKK HHHHHHHHHHHHHHH	49.48	-
565	Phosphorylation	KKPLERESISTTPKC CCCCHHCCCCCCCCH	28.23	29396449
567	Phosphorylation	PLERESISTTPKCFL CCHHCCCCCCCCHHH	35.19	24719451
568	Phosphorylation	LERESISTTPKCFLE CHHCCCCCCCCHHHH	45.51	23312004
569	Phosphorylation	ERESISTTPKCFLEK HHCCCCCCCCHHHHH	17.60	21815630
571	Ubiquitination	ESISTTPKCFLEKAK CCCCCCCCHHHHHHH	35.21	-
585	Phosphorylation	KDKQKKVTGQNSKKK HHHCCCCCCCCCCCC	41.76	17929957
589	Phosphorylation	KKVTGQNSKKKVALE CCCCCCCCCCCEECC	37.65	17929957
599	Phosphorylation	KVALEDKS------- CEECCCCC-------	58.75	21815630

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
22	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DDX52_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 DDX52_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BPL1_HUMAN	HLCS	physical	21988832
PMP22_HUMAN	PMP22	physical	21988832
IMP4_HUMAN	IMP4	physical	26344197
PUM3_HUMAN	KIAA0020	physical	26344197
NOC4L_HUMAN	NOC4L	physical	26344197
NOL10_HUMAN	NOL10	physical	26344197
RL1D1_HUMAN	RSL1D1	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 DDX52_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-15, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-39, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-99, AND MASSSPECTROMETRY.	17525332 [Abstract]