dbPTM

DDX27_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDX27_HUMAN
UniProt AC	Q96GQ7
Protein Name	Probable ATP-dependent RNA helicase DDX27
Gene Name	DDX27
Organism	Homo sapiens (Human).
Sequence Length	796
Subcellular Localization	Nucleus, nucleolus . Chromosome . Associates with 60S and 90S pre-ribosomal particles (PubMed:25825154).
Protein Description	Probable ATP-dependent RNA helicase. Component of the nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3' end formation of ribosomal 47S rRNA. [PubMed: 25825154]
Protein Sequence	MVLAQRRRGGCEKLRAGPQAVLASGSGFCDNMLADLGLIGTIGEDDEVPVEPESDSGDEEEEGPIVLGRRQKALGKNRSADFNPDFVFTEKEGTYDGSWALADVMSQLKKKRAATTLDEKIEKVRKKRKTEDKEAKSGKLEKEKEAKEGSEPKEQEDLQENDEEGSEDEASETDYSSADENILTKADTLKVKDRKKKKKKGQEAGGFFEDASQYDENLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQLEAEEKEMQQSEAQINTAKRLLEKGKEAVVQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILKAQMFAERLAKRNRRAKRARAMPEEEPVRGPAKKQKQGKKSVFDEELTNTSKKALKQYRAGPSFEERKQLGLPHQRRGGNFKSKSRYKRRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Phosphorylation	ADLGLIGTIGEDDEV HHHCCEEECCCCCCC	20.86	24532841
54	Phosphorylation	EVPVEPESDSGDEEE CCCCCCCCCCCCCCC	48.03	29743597
56	Phosphorylation	PVEPESDSGDEEEEG CCCCCCCCCCCCCCC	58.38	29743597
79	Phosphorylation	KALGKNRSADFNPDF HHCCCCCCCCCCCCC	41.40	30266825
89	Phosphorylation	FNPDFVFTEKEGTYD CCCCCEEECCCCCCC	40.63	24732914
95	Phosphorylation	FTEKEGTYDGSWALA EECCCCCCCCCHHHH	29.21	-
106	Phosphorylation	WALADVMSQLKKKRA HHHHHHHHHHHHHHH	32.01	21712546
109	Methylation	ADVMSQLKKKRAATT HHHHHHHHHHHHCCC	48.92	-
109	Acetylation	ADVMSQLKKKRAATT HHHHHHHHHHHHCCC	48.92	26051181
110	Methylation	DVMSQLKKKRAATTL HHHHHHHHHHHCCCH	56.96	-
120	Acetylation	AATTLDEKIEKVRKK HCCCHHHHHHHHHHH	56.69	26051181
120	2-Hydroxyisobutyrylation	AATTLDEKIEKVRKK HCCCHHHHHHHHHHH	56.69	-
130	Phosphorylation	KVRKKRKTEDKEAKS HHHHHCCCCCHHHHC	54.15	20068231
137	Phosphorylation	TEDKEAKSGKLEKEK CCCHHHHCCHHHHHH	48.48	26074081
150	Phosphorylation	EKEAKEGSEPKEQED HHHHHCCCCCHHHHH	52.39	25999147
166	Phosphorylation	QENDEEGSEDEASET HHCCCCCCCCHHHHC	45.19	25849741
171	Phosphorylation	EGSEDEASETDYSSA CCCCCHHHHCCCCCC	38.69	25849741
173	Phosphorylation	SEDEASETDYSSADE CCCHHHHCCCCCCCC	37.43	25137130
175	Phosphorylation	DEASETDYSSADENI CHHHHCCCCCCCCCC	16.37	25849741
176	Phosphorylation	EASETDYSSADENIL HHHHCCCCCCCCCCC	23.12	25849741
177	Phosphorylation	ASETDYSSADENILT HHHCCCCCCCCCCCC	33.25	25849741
184	Phosphorylation	SADENILTKADTLKV CCCCCCCCHHHHHCC	22.01	21406692
212	Phosphorylation	GGFFEDASQYDENLS CCCCCCHHHCCCCCC	41.41	-
226	Phosphorylation	SFQDMNLSRPLLKAI CHHHCCCCHHHHHHH	27.18	20860994
239	Acetylation	AITAMGFKQPTPIQK HHHHCCCCCCCHHHH	50.03	25953088
242	O-linked_Glycosylation	AMGFKQPTPIQKACI HCCCCCCCHHHHHHC	30.45	28510447
246	Acetylation	KQPTPIQKACIPVGL CCCCHHHHHHCCCCC	46.04	26051181
248	Glutathionylation	PTPIQKACIPVGLLG CCHHHHHHCCCCCCC	4.68	22555962
256	Ubiquitination	IPVGLLGKDICACAA CCCCCCCCCEEEHHC	43.84	-
256	Acetylation	IPVGLLGKDICACAA CCCCCCCCCEEEHHC	43.84	26051181
269	Phosphorylation	AATGTGKTAAFALPV HCCCCCHHHHHHHHH	25.27	20068231
283	Acetylation	VLERLIYKPRQAPVT HHHHHCCCCCCCCCE	27.08	26051181
298	Phosphorylation	RVLVLVPTRELGIQV EEEEEEECHHHCCCH	29.33	-
307	Phosphorylation	ELGIQVHSVTRQLAQ HHCCCHHHHHHHHHH	26.74	20068231
309	Phosphorylation	GIQVHSVTRQLAQFC CCCHHHHHHHHHHHC	18.73	21406692
331	Phosphorylation	VGGLDVKSQEAALRA ECCCCCCCHHHHHHH	32.85	-
346	Phosphorylation	APDILIATPGRLIDH CCCEEEECCCHHHHH	21.20	19691289
402	Phosphorylation	HRQTMLFSATMTDEV HHHHHHEEEECCHHH	20.90	20068231
404	Phosphorylation	QTMLFSATMTDEVKD HHHHEEEECCHHHHH	21.29	20068231
406	Phosphorylation	MLFSATMTDEVKDLA HHEEEECCHHHHHHH	25.34	20068231
414	Phosphorylation	DEVKDLASVSLKNPV HHHHHHHHCCCCCCE	21.38	30278072
416	Phosphorylation	VKDLASVSLKNPVRI HHHHHHCCCCCCEEE	31.00	-
418	Acetylation	DLASVSLKNPVRIFV HHHHCCCCCCEEEEE	52.26	25953088
459	Phosphorylation	AIVAALLTRTFTDHV HHHHHHHHCCCCCCH	28.63	20860994
461	Phosphorylation	VAALLTRTFTDHVML HHHHHHCCCCCCHHH	26.17	22210691
463	Phosphorylation	ALLTRTFTDHVMLFT HHHHCCCCCCHHHHH	25.28	22210691
470	Phosphorylation	TDHVMLFTQTKKQAH CCCHHHHHCCHHHHH	31.22	-
472	Phosphorylation	HVMLFTQTKKQAHRM CHHHHHCCHHHHHHH	36.83	-
473	Acetylation	VMLFTQTKKQAHRMH HHHHHCCHHHHHHHH	32.82	26051181
534	Phosphorylation	LDIEGVKTVINFTMP CCCCCCEEEEECCCC	24.98	20068231
539	Phosphorylation	VKTVINFTMPNTIKH CEEEEECCCCCHHHH	27.51	20068231
543	Phosphorylation	INFTMPNTIKHYVHR EECCCCCHHHHHHHH	26.07	20068231
545	Acetylation	FTMPNTIKHYVHRVG CCCCCHHHHHHHHHH	27.18	25953088
563	Phosphorylation	RAGRAGRSVSLVGED CCCCCCCCCCCCCHH	18.36	29759185
565	Phosphorylation	GRAGRSVSLVGEDER CCCCCCCCCCCHHHH	20.70	29759185
598	Acetylation	LPQDVILKFRDKIEK CCHHHHHHHHHHHHH	27.51	26051181
598	Ubiquitination	LPQDVILKFRDKIEK CCHHHHHHHHHHHHH	27.51	-
605	Sumoylation	KFRDKIEKMEKDVYA HHHHHHHHHHHHHHH	56.69	-
605	Sumoylation	KFRDKIEKMEKDVYA HHHHHHHHHHHHHHH	56.69	-
611	Phosphorylation	EKMEKDVYAVLQLEA HHHHHHHHHHHHHHH	10.92	23879269
632	Phosphorylation	QSEAQINTAKRLLEK HHHHHHHHHHHHHHH	34.87	25159151
634	Ubiquitination	EAQINTAKRLLEKGK HHHHHHHHHHHHHCH	41.35	-
634	2-Hydroxyisobutyrylation	EAQINTAKRLLEKGK HHHHHHHHHHHHHCH	41.35	-
641	2-Hydroxyisobutyrylation	KRLLEKGKEAVVQEP HHHHHHCHHHHHCCC	54.27	-
651	Phosphorylation	VVQEPERSWFQTKEE HHCCCCCCCCCCHHH	30.49	25159151
656	Ubiquitination	ERSWFQTKEERKKEK CCCCCCCHHHHHHHH	46.96	-
656	Acetylation	ERSWFQTKEERKKEK CCCCCCCHHHHHHHH	46.96	26051181
666	2-Hydroxyisobutyrylation	RKKEKIAKALQEFDL HHHHHHHHHHHHHHH	53.77	-
695	Phosphorylation	AKKKGEMTAEERSQF HHHHCCCCHHHHHHH	26.98	21406692
706	Ubiquitination	RSQFEILKAQMFAER HHHHHHHHHHHHHHH	42.08	-
738	Acetylation	EPVRGPAKKQKQGKK CCCCCCHHHCCCCCC	59.89	25953088
745	Ubiquitination	KKQKQGKKSVFDEEL HHCCCCCCCCCCHHH	59.69	-
746	Phosphorylation	KQKQGKKSVFDEELT HCCCCCCCCCCHHHC	31.35	25159151
753	Phosphorylation	SVFDEELTNTSKKAL CCCCHHHCHHHHHHH	39.47	23312004
755	Phosphorylation	FDEELTNTSKKALKQ CCHHHCHHHHHHHHH	36.37	21815630
756	Phosphorylation	DEELTNTSKKALKQY CHHHCHHHHHHHHHH	33.94	21815630
757	2-Hydroxyisobutyrylation	EELTNTSKKALKQYR HHHCHHHHHHHHHHH	39.77	-
763	Phosphorylation	SKKALKQYRAGPSFE HHHHHHHHHCCCCHH	10.80	-
766	Phosphorylation	ALKQYRAGPSFEERK HHHHHHCCCCHHHHH	14.91	16565220
768	Phosphorylation	KQYRAGPSFEERKQL HHHHCCCCHHHHHHH	44.35	25159151

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 DDX27_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DDX27_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 DDX27_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCA13_HUMAN	DCAF13	physical	26344197
DKC1_HUMAN	DKC1	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
PESC_HUMAN	PES1	physical	26344197
RBBP6_HUMAN	RBBP6	physical	26344197
RBM19_HUMAN	RBM19	physical	26344197
RBM34_HUMAN	RBM34	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
SRP68_HUMAN	SRP68	physical	26344197
SRP72_HUMAN	SRP72	physical	26344197
LA_HUMAN	SSB	physical	26344197
UT14A_HUMAN	UTP14A	physical	26344197
PESC_HUMAN	PES1	physical	25825154
BOP1_HUMAN	BOP1	physical	25825154

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 DDX27_HUMAN

Related Literatures of Post-Translational Modification

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-79; SER-166; SER-171;TYR-175; SER-176 AND SER-177, AND MASS SPECTROMETRY.	18669648 [Abstract]