dbPTM

DGCR8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DGCR8_HUMAN
UniProt AC	Q8WYQ5
Protein Name	Microprocessor complex subunit DGCR8
Gene Name	DGCR8
Organism	Homo sapiens (Human).
Sequence Length	773
Subcellular Localization	Nucleus . Nucleus, nucleolus . Colocalizes with nucleolin and DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-dense granular patches around the fibrillar center (FC) and granular component (GC). Also detected in the nucleoplasm
Protein Description	Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. [PubMed: 26027739]
Protein Sequence	METDESPSPLPCGPAGEAVMESRARPFQALPREQSPPPPLQTSSGAEVMDVGSGGDGQSELPAEDPFNFYGASLLSKGSFSKGRLLIDPNCSGHSPRTARHAPAVRKFSPDLKLLKDVKISVSFTESCRSKDRKVLYTGAERDVRAECGLLLSPVSGDVHACPFGGSVGDGVGIGGESADKKDEENELDQEKRVEYAVLDELEDFTDNLELDEEGAGGFTAKAIVQRDRVDEEALNFPYEDDFDNDVDALLEEGLCAPKKRRTEEKYGGDSDHPSDGETSVQPMMTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGVPVYLHRESRVVTWSRPYFLGTGSIRKHDPPLSSIPCLHYKKMKDNEEREQSSDLTPSGDVSPVKPLSRSAELEFPLDEPDSMGADPGPPDEKDPLGAEAAPGALGQVKAKVEVCKDESVDLEEFRSYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAESERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVTIDGVTYGSGTASSKKLAKNKAARATLEILIPDFVKQTSEEKPKDSEELEYFNHISIEDSRVYELTSKAGLLSPYQILHECLKRNHGMGDTSIKFEVVPGKNQKSEYVMACGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRESSKMVKQETSDKSVIELQQYAKKNKPNLHILSKLQEEMKRLAEEREETRKKPKMSIVASAQPGGEPLCTVDV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----METDESPSPL -----CCCCCCCCCC	43.71	26552605
6	Phosphorylation	--METDESPSPLPCG --CCCCCCCCCCCCC	33.22	22199227
8	Phosphorylation	METDESPSPLPCGPA CCCCCCCCCCCCCHH	48.63	25159151
22	Phosphorylation	AGEAVMESRARPFQA HHHHHHHHCCCCCCC	17.10	26552605
35	Phosphorylation	QALPREQSPPPPLQT CCCCCCCCCCCCCCC	34.32	21082442
42	Phosphorylation	SPPPPLQTSSGAEVM CCCCCCCCCCCCEEE	32.32	26074081
43	Phosphorylation	PPPPLQTSSGAEVMD CCCCCCCCCCCEEEE	17.51	26074081
44	Phosphorylation	PPPLQTSSGAEVMDV CCCCCCCCCCEEEEC	45.47	28464451
53	Phosphorylation	AEVMDVGSGGDGQSE CEEEECCCCCCCCCC	39.18	25921289
59	Phosphorylation	GSGGDGQSELPAEDP CCCCCCCCCCCCCCC	46.78	28464451
70	Phosphorylation	AEDPFNFYGASLLSK CCCCCCCCCHHHCCC	16.94	27080861
73	Phosphorylation	PFNFYGASLLSKGSF CCCCCCHHHCCCCCC	26.02	24905233
76	Phosphorylation	FYGASLLSKGSFSKG CCCHHHCCCCCCCCC	40.02	27080861
79	Phosphorylation	ASLLSKGSFSKGRLL HHHCCCCCCCCCCEE	30.04	24719451
92	Phosphorylation	LLIDPNCSGHSPRTA EEECCCCCCCCCCHH	46.29	29255136
95	Phosphorylation	DPNCSGHSPRTARHA CCCCCCCCCCHHHCC	21.43	29255136
98	Phosphorylation	CSGHSPRTARHAPAV CCCCCCCHHHCCHHH	31.28	28111955
109	Phosphorylation	APAVRKFSPDLKLLK CHHHHHCCCCCHHHC	22.12	23401153
113	Ubiquitination	RKFSPDLKLLKDVKI HHCCCCCHHHCCCEE	60.19	29967540
123	Phosphorylation	KDVKISVSFTESCRS CCCEEEEEECHHHHC	21.47	23403867
125	Phosphorylation	VKISVSFTESCRSKD CEEEEEECHHHHCCC	21.34	23403867
134	Ubiquitination	SCRSKDRKVLYTGAE HHHCCCCEEEECCCC	46.88	29967540
153	Phosphorylation	AECGLLLSPVSGDVH HHHCCEEECCCCCCE	24.19	25159151
156	Phosphorylation	GLLLSPVSGDVHACP CCEEECCCCCCEECC	32.43	30576142
167	Phosphorylation	HACPFGGSVGDGVGI EECCCCCCCCCCCCC	24.25	27732954
178	Phosphorylation	GVGIGGESADKKDEE CCCCCCCCCCCCCCC	45.07	27251275
259	Sumoylation	EEGLCAPKKRRTEEK HCCCCCCCCCCCCHH	40.15	-
259	Sumoylation	EEGLCAPKKRRTEEK HCCCCCCCCCCCCHH	40.15	-
263	Phosphorylation	CAPKKRRTEEKYGGD CCCCCCCCCHHHCCC	53.15	22210691
267	Phosphorylation	KRRTEEKYGGDSDHP CCCCCHHHCCCCCCC	29.62	26846344
271	Phosphorylation	EEKYGGDSDHPSDGE CHHHCCCCCCCCCCC	40.88	26846344
275	Phosphorylation	GGDSDHPSDGETSVQ CCCCCCCCCCCCCHH	55.62	26846344
279	Phosphorylation	DHPSDGETSVQPMMT CCCCCCCCCHHHHHH	39.46	23927012
280	Phosphorylation	HPSDGETSVQPMMTK CCCCCCCCHHHHHHH	17.91	23927012
286	Phosphorylation	TSVQPMMTKIKTVLK CCHHHHHHHHHHHHH	24.30	23403867
330	Phosphorylation	ESRVVTWSRPYFLGT CCCEEEECCCEEECC	17.63	28851738
333	Phosphorylation	VVTWSRPYFLGTGSI EEEECCCEEECCCCC	15.43	28851738
337	Phosphorylation	SRPYFLGTGSIRKHD CCCEEECCCCCCCCC	29.87	30108239
339	Phosphorylation	PYFLGTGSIRKHDPP CEEECCCCCCCCCCC	21.03	30108239
356	Acetylation	SIPCLHYKKMKDNEE HCCEEEEECCCCHHH	35.33	26051181
367	Phosphorylation	DNEEREQSSDLTPSG CHHHHHHHCCCCCCC	22.52	30266825
368	Phosphorylation	NEEREQSSDLTPSGD HHHHHHHCCCCCCCC	36.01	30266825
371	Phosphorylation	REQSSDLTPSGDVSP HHHHCCCCCCCCCCC	22.02	30266825
373	Phosphorylation	QSSDLTPSGDVSPVK HHCCCCCCCCCCCCC	42.25	29255136
377	Phosphorylation	LTPSGDVSPVKPLSR CCCCCCCCCCCCCCC	28.81	29255136
380	Ubiquitination	SGDVSPVKPLSRSAE CCCCCCCCCCCCCEE	43.56	29967540
383	Phosphorylation	VSPVKPLSRSAELEF CCCCCCCCCCEEEEC	32.49	30266825
385	Phosphorylation	PVKPLSRSAELEFPL CCCCCCCCEEEECCC	23.79	25159151
397	Phosphorylation	FPLDEPDSMGADPGP CCCCCCCCCCCCCCC	29.81	21815630
424	Sumoylation	PGALGQVKAKVEVCK CCCHHHHEEEEEECC	34.30	28112733
424	Ubiquitination	PGALGQVKAKVEVCK CCCHHHHEEEEEECC	34.30	29967540
431	Ubiquitination	KAKVEVCKDESVDLE EEEEEECCCCCCCHH	70.48	29967540
434	Phosphorylation	VEVCKDESVDLEEFR EEECCCCCCCHHHHH	30.94	25849741
474	Ubiquitination	FNREMKRKQAESERP HHHHHHHHHHHHCCC	48.63	29967540
488	Ubiquitination	PILPANQKLITLSVQ CCCCCCCEEEEEEEC	41.48	29967540
493	Phosphorylation	NQKLITLSVQDAPTK CCEEEEEEECCCCCC	14.75	-
500	Sumoylation	SVQDAPTKKEFVINP EECCCCCCCEEEECC	49.61	28112733
501	Ubiquitination	VQDAPTKKEFVINPN ECCCCCCCEEEECCC	59.88	-
545	Phosphorylation	PSEPFGASVTIDGVT CCCCCCEEEEECCEE	21.85	-
547	Phosphorylation	EPFGASVTIDGVTYG CCCCEEEEECCEEEC	15.74	-
582	Ubiquitination	ILIPDFVKQTSEEKP HHCHHHHHHCCCCCC	48.10	29967540
585	Phosphorylation	PDFVKQTSEEKPKDS HHHHHHCCCCCCCCH	41.06	24719451
597	Phosphorylation	KDSEELEYFNHISIE CCHHHHHHEECCEEC	23.47	27642862
607	Ubiquitination	HISIEDSRVYELTSK CCEECCCCEEEHHCC	47.56	29967540
609	Phosphorylation	SIEDSRVYELTSKAG EECCCCEEEHHCCCC	12.24	27642862
614	Ubiquitination	RVYELTSKAGLLSPY CEEEHHCCCCCCCHH	41.04	33845483
619	Phosphorylation	TSKAGLLSPYQILHE HCCCCCCCHHHHHHH	26.97	28122231
626	Ubiquitination	SPYQILHECLKRNHG CHHHHHHHHHHHCCC	37.79	29967540
629	Acetylation	QILHECLKRNHGMGD HHHHHHHHHCCCCCC	63.91	25953088
640	Acetylation	GMGDTSIKFEVVPGK CCCCCEEEEEEECCC	34.93	25953088
640	Ubiquitination	GMGDTSIKFEVVPGK CCCCCEEEEEEECCC	34.93	29967540
647	Ubiquitination	KFEVVPGKNQKSEYV EEEEECCCCCCCEEE	50.57	33845483
650	Acetylation	VVPGKNQKSEYVMAC EECCCCCCCEEEEEC	55.43	26051181
659	Ubiquitination	EYVMACGKHTVRGWC EEEEECCCCCHHHHH	35.67	29967540
680	Ubiquitination	KQLASQKILQLLHPH HHHHHHHHHHHHCHH	1.99	29967540
690	Ubiquitination	LLHPHVKNWGSLLRM HHCHHHHCHHHHHHH	47.45	33845483
691	Ubiquitination	LHPHVKNWGSLLRMY HCHHHHCHHHHHHHH	7.64	29967540
693	Ubiquitination	PHVKNWGSLLRMYGR HHHHCHHHHHHHHCH	18.82	29967540
702	Phosphorylation	LRMYGRESSKMVKQE HHHHCHHHHCHHCCC	33.62	29083192
703	Phosphorylation	RMYGRESSKMVKQET HHHCHHHHCHHCCCC	21.73	29083192
707	Sumoylation	RESSKMVKQETSDKS HHHHCHHCCCCCCCH	38.63	-
707	Sumoylation	RESSKMVKQETSDKS HHHHCHHCCCCCCCH	38.63	25218447
710	Phosphorylation	SKMVKQETSDKSVIE HCHHCCCCCCCHHHH	39.47	23312004
711	Phosphorylation	KMVKQETSDKSVIEL CHHCCCCCCCHHHHH	42.14	28985074
713	Ubiquitination	VKQETSDKSVIELQQ HCCCCCCCHHHHHHH	46.52	29967540
714	Phosphorylation	KQETSDKSVIELQQY CCCCCCCHHHHHHHH	33.06	25159151
723	Ubiquitination	IELQQYAKKNKPNLH HHHHHHHHHCCCCHH	52.52	33845483
724	Ubiquitination	ELQQYAKKNKPNLHI HHHHHHHHCCCCHHH	63.13	29967540
726	Ubiquitination	QQYAKKNKPNLHILS HHHHHHCCCCHHHHH	44.13	29967540

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
153	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
267	Y	Phosphorylation	Kinase	ABL1	P00520	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DGCR8_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 DGCR8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUCL_HUMAN	NCL	physical	17765891
GRP78_HUMAN	HSPA5	physical	17765891
HSP7C_HUMAN	HSPA8	physical	17765891
HNRPR_HUMAN	HNRNPR	physical	17765891
DDX5_HUMAN	DDX5	physical	17765891
DDX17_HUMAN	DDX17	physical	17765891
FUS_HUMAN	FUS	physical	17765891
HNRH1_HUMAN	HNRNPH1	physical	17765891
DHX9_HUMAN	DHX9	physical	17765891
HNRPU_HUMAN	HNRNPU	physical	17765891
ILF3_HUMAN	ILF3	physical	17765891
RNC_HUMAN	DROSHA	physical	17765891
A4_HUMAN	APP	physical	21832049
PRP4_HUMAN	PRPF4	physical	22939629
MARE2_HUMAN	MAPRE2	physical	22939629
NAT10_HUMAN	NAT10	physical	22939629
PLEK2_HUMAN	PLEK2	physical	22939629
RPRD2_HUMAN	RPRD2	physical	22939629
FLII_HUMAN	FLII	physical	22939629
CDN2A_HUMAN	CDKN2A	physical	24778252
ARF_HUMAN	CDKN2A	physical	24778252
RNC_HUMAN	DROSHA	physical	24778252
ERH_HUMAN	ERH	physical	24778252
MK01_HUMAN	MAPK1	physical	24778252
ANM1_HUMAN	PRMT1	physical	24778252
P5CR3_HUMAN	PYCRL	physical	24778252
RAE1L_HUMAN	RAE1	physical	24778252
HNRL1_HUMAN	HNRNPUL1	physical	26496610
RNC_HUMAN	DROSHA	physical	26496610
KIF15_HUMAN	KIF15	physical	26496610
TLN2_HUMAN	TLN2	physical	26496610
RNC_HUMAN	DROSHA	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
ZNF7_HUMAN	ZNF7	physical	28514442
CENPI_HUMAN	CENPI	physical	28514442
CENPR_HUMAN	ITGB3BP	physical	28514442
CENPO_HUMAN	CENPO	physical	28514442
SHQ1_HUMAN	SHQ1	physical	28514442
CENPC_HUMAN	CENPC	physical	28514442
CENPN_HUMAN	CENPN	physical	28514442
CENPU_HUMAN	CENPU	physical	28514442
ZN189_HUMAN	ZNF189	physical	28514442
PAPD5_HUMAN	PAPD5	physical	28514442
ZNF70_HUMAN	ZNF70	physical	28514442
CENPQ_HUMAN	CENPQ	physical	28514442
ZN483_HUMAN	ZNF483	physical	28514442
ZN800_HUMAN	ZNF800	physical	28514442
NSA2_HUMAN	NSA2	physical	28514442
NSD2_HUMAN	WHSC1	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
BEND7_HUMAN	BEND7	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
TTF1_HUMAN	TTF1	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
KNOP1_HUMAN	KNOP1	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RALY_HUMAN	RALY	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
MPP10_HUMAN	MPHOSPH10	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
CC137_HUMAN	CCDC137	physical	28514442
ZN689_HUMAN	ZNF689	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
ZFP62_HUMAN	ZFP62	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
DDX10_HUMAN	DDX10	physical	28514442
UTP23_HUMAN	UTP23	physical	28514442
ZCHC7_HUMAN	ZCCHC7	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
ZNF22_HUMAN	ZNF22	physical	28514442
RL17_HUMAN	RPL17	physical	28514442
MAK16_HUMAN	MAK16	physical	28514442
STAU2_HUMAN	STAU2	physical	28514442
LAR1B_HUMAN	LARP1B	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
TDIF2_HUMAN	DNTTIP2	physical	28514442
ZN771_HUMAN	ZNF771	physical	28514442
NVL_HUMAN	NVL	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
MOV10_HUMAN	MOV10	physical	28514442
DDX18_HUMAN	DDX18	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
SURF6_HUMAN	SURF6	physical	28514442
FCF1_HUMAN	FCF1	physical	28514442
PINX1_HUMAN	PINX1	physical	28514442
SPT2_HUMAN	SPTY2D1	physical	28514442
ZN646_HUMAN	ZNF646	physical	28514442
PK1IP_HUMAN	PAK1IP1	physical	28514442
RLA2_HUMAN	RPLP2	physical	28514442
SRPK1_HUMAN	SRPK1	physical	28514442
CENPH_HUMAN	CENPH	physical	28514442
ZN777_HUMAN	ZNF777	physical	28514442
CTCF_HUMAN	CTCF	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
NOL10_HUMAN	NOL10	physical	28514442
RS13_HUMAN	RPS13	physical	28514442
REPI1_HUMAN	REPIN1	physical	28514442
PRKRA_HUMAN	PRKRA	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
RL10A_HUMAN	RPL10A	physical	28514442
WDR12_HUMAN	WDR12	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
DDX56_HUMAN	DDX56	physical	28514442
MK67I_HUMAN	NIFK	physical	28514442
DDX54_HUMAN	DDX54	physical	28514442
POP1_HUMAN	POP1	physical	28514442
RS8_HUMAN	RPS8	physical	28514442
HERC5_HUMAN	HERC5	physical	28514442
NOC3L_HUMAN	NOC3L	physical	28514442
NR2E1_HUMAN	NR2E1	physical	26965827

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 DGCR8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-271 AND SER-275, ANDMASS SPECTROMETRY.	19690332 [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-92; SER-95; SER-109;SER-271; SER-275 AND SER-377, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	18220336 [Abstract]