dbPTM

RU17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RU17_HUMAN
UniProt AC	P08621
Protein Name	U1 small nuclear ribonucleoprotein 70 kDa
Gene Name	SNRNP70
Organism	Homo sapiens (Human).
Sequence Length	437
Subcellular Localization	Nucleus. Nucleus speckle. Nucleus, nucleoplasm. Colocalizes with SCNM1 and LUC7L2 in nuclear speckles..
Protein Description	Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA..
Protein Sequence	MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRHSGRDDTSRYDERPGPSPLPHRDRDRDRERERRERSRERDKERERRRSRSRDRRRRSRSRDKEERRRSRERSKDKDRDRKRRSSRSRERARRERERKEELRGGGGDMAEPSEAGDAPPDDGPPGELGPDGPDGPEEKGRDRDRERRRSHRSERERRRDRDRDRDRDREHKRGERGSERGRDEARGGGGGQDNGLEGLGNDSRDMYMESEGGDGYLAPENGYLMEAAPE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTQFLPPNL ------CCCCCCHHH	28.20	22223895
21	Phosphorylation	APRDPIPYLPPLEKL CCCCCCCCCCCHHHC	32.34	28152594
27 (in isoform 2)	Ubiquitination	-	75.01	21890473
27 (in isoform 3)	Ubiquitination	-	75.01	21890473
27	Acetylation	PYLPPLEKLPHEKHH CCCCCHHHCCCCCCC	75.01	23236377
27 (in isoform 1)	Ubiquitination	-	75.01	21890473
27	Ubiquitination	PYLPPLEKLPHEKHH CCCCCHHHCCCCCCC	75.01	21890473
32	Acetylation	LEKLPHEKHHNQPYC HHHCCCCCCCCCCCC	47.32	21466224
38	Phosphorylation	EKHHNQPYCGIAPYI CCCCCCCCCCCHHHH	8.11	28152594
39	Glutathionylation	KHHNQPYCGIAPYIR CCCCCCCCCCHHHHH	3.96	22555962
58	O-linked_Glycosylation	PRDAPPPTRAETREE CCCCCCCCHHHHHHH	48.57	28510447
84	Phosphorylation	RRQQEVETELKMWDP HHHHHHHHHHHHCCC	52.36	21406692
87 (in isoform 2)	Ubiquitination	-	31.54	21890473
87 (in isoform 1)	Ubiquitination	-	31.54	21890473
87 (in isoform 3)	Ubiquitination	-	31.54	21890473
87	Ubiquitination	QEVETELKMWDPHND HHHHHHHHHCCCCCC	31.54	21906983
87	Acetylation	QEVETELKMWDPHND HHHHHHHHHCCCCCC	31.54	26051181
103	Ubiquitination	NAQGDAFKTLFVARV CCCCHHHHHEEEEEE	46.14	21890473
103 (in isoform 3)	Ubiquitination	-	46.14	21890473
103 (in isoform 1)	Ubiquitination	-	46.14	21890473
103 (in isoform 2)	Ubiquitination	-	46.14	21890473
103	Acetylation	NAQGDAFKTLFVARV CCCCHHHHHEEEEEE	46.14	26051181
112	Phosphorylation	LFVARVNYDTTESKL EEEEEECCCCCHHHH	16.29	29116813
114	Phosphorylation	VARVNYDTTESKLRR EEEECCCCCHHHHHH	23.31	29116813
115	Phosphorylation	ARVNYDTTESKLRRE EEECCCCCHHHHHHH	35.05	29116813
117	Phosphorylation	VNYDTTESKLRREFE ECCCCCHHHHHHHEE	34.59	21815630
118	Ubiquitination	NYDTTESKLRREFEV CCCCCHHHHHHHEEE	39.52	19608861
118	2-Hydroxyisobutyrylation	NYDTTESKLRREFEV CCCCCHHHHHHHEEE	39.52	-
118	Acetylation	NYDTTESKLRREFEV CCCCCHHHHHHHEEE	39.52	19608861
126	Phosphorylation	LRREFEVYGPIKRIH HHHHEEEECCEEEEE	15.24	23401153
130 (in isoform 2)	Ubiquitination	-	48.73	21890473
130 (in isoform 1)	Ubiquitination	-	48.73	21890473
130	Acetylation	FEVYGPIKRIHMVYS EEEECCEEEEEEEEE	48.73	25953088
130	Methylation	FEVYGPIKRIHMVYS EEEECCEEEEEEEEE	48.73	-
130	Ubiquitination	FEVYGPIKRIHMVYS EEEECCEEEEEEEEE	48.73	21890473
130 (in isoform 3)	Ubiquitination	-	48.73	21890473
136	Phosphorylation	IKRIHMVYSKRSGKP EEEEEEEEECCCCCC	10.82	25839225
137	Phosphorylation	KRIHMVYSKRSGKPR EEEEEEEECCCCCCC	15.35	12548559
140	Phosphorylation	HMVYSKRSGKPRGYA EEEEECCCCCCCEEE	55.71	22817900
146	Phosphorylation	RSGKPRGYAFIEYEH CCCCCCEEEEEEEEC	10.30	28152594
151	Phosphorylation	RGYAFIEYEHERDMH CEEEEEEEECHHHHH	20.12	28152594
162	Acetylation	RDMHSAYKHADGKKI HHHHHHHCCCCCCEE	31.84	23749302
180	Methylation	RVLVDVERGRTVKGW EEEEECCCCCEECCC	39.48	12018419
185	Ubiquitination	VERGRTVKGWRPRRL CCCCCEECCCCCCCC	52.74	-
199	Phosphorylation	LGGGLGGTRRGGADV CCCCCCCCCCCCCCC	18.52	21406692
201	Methylation	GGLGGTRRGGADVNI CCCCCCCCCCCCCEE	47.97	12018431
211	Phosphorylation	ADVNIRHSGRDDTSR CCCEEECCCCCCCCC	26.19	28985074
216	Phosphorylation	RHSGRDDTSRYDERP ECCCCCCCCCCCCCC	21.28	23927012
217	Phosphorylation	HSGRDDTSRYDERPG CCCCCCCCCCCCCCC	35.52	23927012
219	Phosphorylation	GRDDTSRYDERPGPS CCCCCCCCCCCCCCC	23.17	23927012
226	Phosphorylation	YDERPGPSPLPHRDR CCCCCCCCCCCCCCC	45.01	29255136
226	O-linked_Glycosylation	YDERPGPSPLPHRDR CCCCCCCCCCCCCCC	45.01	OGP
245	Phosphorylation	ERERRERSRERDKER HHHHHHHHHHHHHHH	33.47	17081983
250 (in isoform 4)	Ubiquitination	-	65.96	21906983
257	Phosphorylation	KERERRRSRSRDRRR HHHHHHHHHHHHHHH	32.56	20068231
259	Phosphorylation	RERRRSRSRDRRRRS HHHHHHHHHHHHHHH	39.52	20068231
266	Phosphorylation	SRDRRRRSRSRDKEE HHHHHHHHHHHHHHH	32.56	30576142
268	Phosphorylation	DRRRRSRSRDKEERR HHHHHHHHHHHHHHH	46.18	23882029
277	Phosphorylation	DKEERRRSRERSKDK HHHHHHHHHHHHHHH	36.36	-
281	Phosphorylation	RRRSRERSKDKDRDR HHHHHHHHHHHHHHH	40.22	24144214
292	Phosphorylation	DRDRKRRSSRSRERA HHHHHHHHHHHHHHH	33.85	26657352
293	Phosphorylation	RDRKRRSSRSRERAR HHHHHHHHHHHHHHH	32.25	20068231
295	Phosphorylation	RKRRSSRSRERARRE HHHHHHHHHHHHHHH	40.20	26657352
310	Methylation	RERKEELRGGGGDMA HHHHHHHCCCCCCCC	45.02	115917365
320	Phosphorylation	GGDMAEPSEAGDAPP CCCCCCCCCCCCCCC	31.42	25159151
337 (in isoform 2)	Ubiquitination	-	56.88	21890473
346	Acetylation	GPDGPEEKGRDRDRE CCCCCCCCCCHHHHH	58.55	26051181
346	Methylation	GPDGPEEKGRDRDRE CCCCCCCCCCHHHHH	58.55	117839601
346 (in isoform 1)	Ubiquitination	-	58.55	21890473
346	Ubiquitination	GPDGPEEKGRDRDRE CCCCCCCCCCHHHHH	58.55	2190698
346	Sumoylation	GPDGPEEKGRDRDRE CCCCCCCCCCHHHHH	58.55	28112733
357	Phosphorylation	RDRERRRSHRSERER HHHHHHHHHHHHHHH	22.80	20068231
360	Phosphorylation	ERRRSHRSERERRRD HHHHHHHHHHHHHHH	35.27	20068231
385	Phosphorylation	HKRGERGSERGRDEA HHHCCCCHHHCCCCC	30.27	30576142
393	Methylation	ERGRDEARGGGGGQD HHCCCCCCCCCCCCC	42.09	115917369
410	Phosphorylation	LEGLGNDSRDMYMES CCCCCCCCCCEEECC	33.89	19664994
414	Phosphorylation	GNDSRDMYMESEGGD CCCCCCEEECCCCCC	11.30	26074081
417	Phosphorylation	SRDMYMESEGGDGYL CCCEEECCCCCCCEE	25.63	28348404

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
226	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RU17_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 RU17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPSF5_HUMAN	NUDT21	physical	14561889
SRSF1_HUMAN	SRSF1	physical	9685421
RU1C_HUMAN	SNRPC	physical	9826776
SRPK1_HUMAN	SRPK1	physical	12417631
FBW1A_HUMAN	BTRC	physical	11850407
SKP1_HUMAN	SKP1	physical	11850407
CUL1_HUMAN	CUL1	physical	11850407
A4_HUMAN	APP	physical	21832049
SMD3_HUMAN	SNRPD3	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
RUXE_HUMAN	SNRPE	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
SRSF9_HUMAN	SRSF9	physical	22939629
SF3A3_HUMAN	SF3A3	physical	22939629
THIOM_HUMAN	TXN2	physical	22939629
UBQL1_HUMAN	UBQLN1	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
TPM4_HUMAN	TPM4	physical	22939629
CHERP_HUMAN	CHERP	physical	22365833
ANM5_HUMAN	PRMT5	physical	22365833
SRPK2_HUMAN	SRPK2	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
ARGL1_HUMAN	ARGLU1	physical	26344197
LC7L2_HUMAN	LUC7L2	physical	26344197
ANM1_HUMAN	PRMT1	physical	26344197
PRP19_HUMAN	PRPF19	physical	26344197
PR40A_HUMAN	PRPF40A	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
RBM39_HUMAN	RBM39	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RU2B_HUMAN	SNRPB2	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
SMD2_HUMAN	SNRPD2	physical	26344197
SRS11_HUMAN	SRSF11	physical	26344197
SRSF3_HUMAN	SRSF3	physical	26344197
TFP11_HUMAN	TFIP11	physical	26344197
RMXL1_HUMAN	RBMXL1	physical	28514442
CMTR2_HUMAN	CMTR2	physical	28514442
GEMI7_HUMAN	GEMIN7	physical	28514442
SMN_HUMAN	SMN1	physical	28514442
GEMI4_HUMAN	GEMIN4	physical	28514442
KLHL8_HUMAN	KLHL8	physical	28514442
SNRPA_HUMAN	SNRPA	physical	28514442
GEMI5_HUMAN	GEMIN5	physical	28514442
SMD2_HUMAN	SNRPD2	physical	28514442
MEPCE_HUMAN	MEPCE	physical	28514442
RSMB_HUMAN	SNRPB	physical	28514442
SMD1_HUMAN	SNRPD1	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
SMD3_HUMAN	SNRPD3	physical	28514442
SRSF8_HUMAN	SRSF8	physical	28514442
RU1C_HUMAN	SNRPC	physical	28514442
TGS1_HUMAN	TGS1	physical	28514442
MKRN1_HUMAN	MKRN1	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
PRC2A_HUMAN	PRRC2A	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
PHAX_HUMAN	PHAX	physical	28514442
SFR19_HUMAN	SCAF1	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
FOXP1_HUMAN	FOXP1	physical	28514442
GTPB1_HUMAN	GTPBP1	physical	28514442
CLK2_HUMAN	CLK2	physical	28514442
RT09_HUMAN	MRPS9	physical	28514442
SCAFB_HUMAN	SCAF11	physical	28514442
RT18C_HUMAN	MRPS18C	physical	28514442
SLTM_HUMAN	SLTM	physical	28514442
RU2B_HUMAN	SNRPB2	physical	28514442
PRC2C_HUMAN	PRRC2C	physical	28514442
RT31_HUMAN	MRPS31	physical	28514442
RT35_HUMAN	MRPS35	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
SRSF1_HUMAN	SRSF1	physical	28514442
TOE1_HUMAN	TOE1	physical	28514442
ZC3HE_HUMAN	ZC3H14	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
PTCD3_HUMAN	PTCD3	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
YTDC1_HUMAN	YTHDC1	physical	28514442
CI114_HUMAN	C9orf114	physical	28514442
TRA2B_HUMAN	TRA2B	physical	28514442
NOP10_HUMAN	NOP10	physical	28514442
PINX1_HUMAN	PINX1	physical	28514442
MKRN2_HUMAN	MKRN2	physical	28514442
RT26_HUMAN	MRPS26	physical	28514442
RPP40_HUMAN	RPP40	physical	28514442
RT07_HUMAN	MRPS7	physical	28514442
NCBP1_HUMAN	NCBP1	physical	28514442
CC137_HUMAN	CCDC137	physical	28514442
RT10_HUMAN	MRPS10	physical	28514442
RT14_HUMAN	MRPS14	physical	28514442
LARP7_HUMAN	LARP7	physical	28514442
KNOP1_HUMAN	KNOP1	physical	28514442
WDR33_HUMAN	WDR33	physical	28514442
CDC5L_HUMAN	CDC5L	physical	28514442
POP1_HUMAN	POP1	physical	28514442
SRPK2_HUMAN	SRPK2	physical	28514442
RT33_HUMAN	MRPS33	physical	28514442
RT22_HUMAN	MRPS22	physical	28514442
LAR1B_HUMAN	LARP1B	physical	28514442
RM15_HUMAN	MRPL15	physical	28514442
RALY_HUMAN	RALY	physical	28514442
RT29_HUMAN	DAP3	physical	28514442
PABP1_HUMAN	PABPC1	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
RL26_HUMAN	RPL26	physical	28514442

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 RU17_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-118 AND LYS-162, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-226, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-410, AND MASSSPECTROMETRY.	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-226; SER-320 ANDSER-410, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-226 AND SER-410, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASSSPECTROMETRY.	16964243 [Abstract]
"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-226; SER-266; SER-268;SER-320 AND SER-410, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.	15144186 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-126, AND MASSSPECTROMETRY.	18083107 [Abstract]