POP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: POP1_HUMAN
• UniProt AC: Q99575
• Protein Name: Ribonucleases P/MRP protein subunit POP1
• Gene Name: POP1
• Organism: Homo sapiens (Human).
• Sequence Length: 1024
• Subcellular Localization: Nucleus, nucleolus.
• Protein Description: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP..
• Protein Sequence: MSNAKERKHAKKMRNQPTNVTLSSGFVADRGVKHHSGGEKPFQAQKQEPHPGTSRQRQTRVNPHSLPDPEVNEQSSSKGMFRKKGGWKAGPEGTSQEIPKYITASTFAQARAAEISAMLKAVTQKSSNSLVFQTLPRHMRRRAMSHNVKRLPRRLQEIAQKEAEKAVHQKKEHSKNKCHKARRCHMNRTLEFNRRQKKNIWLETHIWHAKRFHMVKKWGYCLGERPTVKSHRACYRAMTNRCLLQDLSYYCCLELKGKEEEILKALSGMCNIDTGLTFAAVHCLSGKRQGSLVLYRVNKYPREMLGPVTFIWKSQRTPGDPSESRQLWIWLHPTLKQDILEEIKAACQCVEPIKSAVCIADPLPTPSQEKSQTELPDEKIGKKRKRKDDGENAKPIKKIIGDGTRDPCLPYSWISPTTGIIISDLTMEMNRFRLIGPLSHSILTEAIKAASVHTVGEDTEETPHRWWIETCKKPDSVSLHCRQEAIFELLGGITSPAEIPAGTILGLTVGDPRINLPQKKSKALPNPEKCQDNEKVRQLLLEGVPVECTHSFIWNQDICKSVTENKISDQDLNRMRSELLVPGSQLILGPHESKIPILLIQQPGKVTGEDRLGWGSGWDVLLPKGWGMAFWIPFIYRGVRVGGLKESAVHSQYKRSPNVPGDFPDCPAGMLFAEEQAKNLLEKYKRRPPAKRPNYVKLGTLAPFCCPWEQLTQDWESRVQAYEEPSVASSPNGKESDLRRSEVPCAPMPKKTHQPSDEVGTSIEHPREAEEVMDAGCQESAGPERITDQEASENHVAATGSHLCVLRSRKLLKQLSAWCGPSSEDSRGGRRAPGRGQQGLTREACLSILGHFPRALVWVSLSLLSKGSPEPHTMICVPAKEDFLQLHEDWHYCGPQESKHSDPFRSKILKQKEKKKREKRQKPGRASSDGPAGEEPVAGQEALTLGLWSGPLPRVTLHCSRTLLGFVTQGDFSMAVGCGEALGFVSLTGLLDMLSSQPAAQRGLVLLRPPASLQYRFARIAIEV

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	KKMRNQPTNVTLSSG HHHCCCCCCCEECCC	32.34	20068231
21	O-linked_Glycosylation	RNQPTNVTLSSGFVA CCCCCCCEECCCCCC	24.00	31373491
21	Phosphorylation	RNQPTNVTLSSGFVA CCCCCCCEECCCCCC	24.00	20068231
23	Phosphorylation	QPTNVTLSSGFVADR CCCCCEECCCCCCCC	21.03	20068231
24	Phosphorylation	PTNVTLSSGFVADRG CCCCEECCCCCCCCC	39.09	21815630
30	Methylation	SSGFVADRGVKHHSG CCCCCCCCCCCCCCC	41.91	97812581
36	Phosphorylation	DRGVKHHSGGEKPFQ CCCCCCCCCCCCCCC	48.49	-
40	Acetylation	KHHSGGEKPFQAQKQ CCCCCCCCCCCCCCC	55.17	23954790
46	Acetylation	EKPFQAQKQEPHPGT CCCCCCCCCCCCCCC	60.69	19608861
53	Phosphorylation	KQEPHPGTSRQRQTR CCCCCCCCCCCCCCC	25.78	20068231
54	Phosphorylation	QEPHPGTSRQRQTRV CCCCCCCCCCCCCCC	32.12	20068231
65	Phosphorylation	QTRVNPHSLPDPEVN CCCCCCCCCCCCCCC	42.74	25159151
75	Phosphorylation	DPEVNEQSSSKGMFR CCCCCCCCCCCCCCC	30.33	25159151
77	Phosphorylation	EVNEQSSSKGMFRKK CCCCCCCCCCCCCCC	38.18	21712546
78	Acetylation	VNEQSSSKGMFRKKG CCCCCCCCCCCCCCC	57.24	26051181
94	Phosphorylation	WKAGPEGTSQEIPKY CCCCCCCCCCCCCCH	26.10	25627689
95	Phosphorylation	KAGPEGTSQEIPKYI CCCCCCCCCCCCCHH	36.35	21815630
100	Acetylation	GTSQEIPKYITASTF CCCCCCCCHHCHHHH	55.75	26051181
100	Ubiquitination	GTSQEIPKYITASTF CCCCCCCCHHCHHHH	55.75	-
105	Phosphorylation	IPKYITASTFAQARA CCCHHCHHHHHHHHH	18.53	28555341
116	Phosphorylation	QARAAEISAMLKAVT HHHHHHHHHHHHHHH	10.11	28555341
129	Phosphorylation	VTQKSSNSLVFQTLP HHHHCCCCCHHHCHH	28.05	28555341
134	Phosphorylation	SNSLVFQTLPRHMRR CCCCHHHCHHHHHHH	27.54	28555341
137	Methylation	LVFQTLPRHMRRRAM CHHHCHHHHHHHHHH	39.07	115488263
145	Phosphorylation	HMRRRAMSHNVKRLP HHHHHHHHHHHHHHH	15.78	24719451
161	Acetylation	RLQEIAQKEAEKAVH HHHHHHHHHHHHHHH	50.28	26051181
189	Phosphorylation	RRCHMNRTLEFNRRQ HHHHHCHHHHHHHHH	26.15	21815630
204	Phosphorylation	KKNIWLETHIWHAKR HCCEEEEEEEHHHHH	19.25	-
274	Phosphorylation	SGMCNIDTGLTFAAV HCCCCCCCCCCEEEE	30.23	30387612
291	Phosphorylation	LSGKRQGSLVLYRVN HCCCCCCCEEEEEEC	13.63	23898821
295	Phosphorylation	RQGSLVLYRVNKYPR CCCCEEEEEECCCCH	12.68	30387612
314	Phosphorylation	PVTFIWKSQRTPGDP CEEEEEECCCCCCCC	15.19	20363803
317	Phosphorylation	FIWKSQRTPGDPSES EEEECCCCCCCCHHH	24.80	20363803
322	Phosphorylation	QRTPGDPSESRQLWI CCCCCCCHHHHHHEE	53.60	21406692
324	Phosphorylation	TPGDPSESRQLWIWL CCCCCHHHHHHEEEC	29.66	21406692
344	Ubiquitination	QDILEEIKAACQCVE HHHHHHHHHHHHCCC	32.96	-
355	Phosphorylation	QCVEPIKSAVCIADP HCCCCCCCCEEEECC	27.01	20068231
365	Phosphorylation	CIADPLPTPSQEKSQ EEECCCCCCCCCCCC	43.16	17525332
367	Phosphorylation	ADPLPTPSQEKSQTE ECCCCCCCCCCCCCC	54.15	25159151
371	Phosphorylation	PTPSQEKSQTELPDE CCCCCCCCCCCCCHH	41.40	17525332
373	Phosphorylation	PSQEKSQTELPDEKI CCCCCCCCCCCHHHH	46.72	23663014
379	Sumoylation	QTELPDEKIGKKRKR CCCCCHHHHCCCCCC	65.23	-
379	Ubiquitination	QTELPDEKIGKKRKR CCCCCHHHHCCCCCC	65.23	-
379	Acetylation	QTELPDEKIGKKRKR CCCCCHHHHCCCCCC	65.23	26051181
404	Phosphorylation	KKIIGDGTRDPCLPY CHHCCCCCCCCCCCC	36.32	17924679
454	Phosphorylation	IKAASVHTVGEDTEE HHHHCCEECCCCCCC	28.22	20071362
535	Acetylation	EKCQDNEKVRQLLLE HHCCCCHHHHHHHHC	49.31	26051181
566	Acetylation	CKSVTENKISDQDLN HHHHHCCCCCHHHHH	37.04	26051181
566	Ubiquitination	CKSVTENKISDQDLN HHHHHCCCCCHHHHH	37.04	21906983
568	Phosphorylation	SVTENKISDQDLNRM HHHCCCCCHHHHHHH	30.72	20068231
577	Phosphorylation	QDLNRMRSELLVPGS HHHHHHHHHHCCCCC	24.21	23186163
584	Phosphorylation	SELLVPGSQLILGPH HHHCCCCCEEEECCC	18.75	17525332
593	Phosphorylation	LILGPHESKIPILLI EEECCCCCCCCEEEE	32.62	23186163
605	Ubiquitination	LLIQQPGKVTGEDRL EEECCCCCCCCCCCC	43.22	2190698
636	Phosphorylation	AFWIPFIYRGVRVGG HHHHHHHHCCCCCCC	11.16	25867546
645	Acetylation	GVRVGGLKESAVHSQ CCCCCCCHHHHHHHH	53.55	26051181
654	Ubiquitination	SAVHSQYKRSPNVPG HHHHHHHCCCCCCCC	38.47	-
654	2-Hydroxyisobutyrylation	SAVHSQYKRSPNVPG HHHHHHHCCCCCCCC	38.47	-
656	Phosphorylation	VHSQYKRSPNVPGDF HHHHHCCCCCCCCCC	19.37	27050516
666	Glutathionylation	VPGDFPDCPAGMLFA CCCCCCCCCHHHHCC	2.24	22555962
722	Phosphorylation	WESRVQAYEEPSVAS HHHHHHHHHCCCCCC	12.06	22167270
726	Phosphorylation	VQAYEEPSVASSPNG HHHHHCCCCCCCCCC	33.33	23401153
729	Phosphorylation	YEEPSVASSPNGKES HHCCCCCCCCCCCHH	44.14	29255136
730	Phosphorylation	EEPSVASSPNGKESD HCCCCCCCCCCCHHH	16.79	19664994
734	Ubiquitination	VASSPNGKESDLRRS CCCCCCCCHHHCCCC	61.76	-
734	Acetylation	VASSPNGKESDLRRS CCCCCCCCHHHCCCC	61.76	26051181
736	Phosphorylation	SSPNGKESDLRRSEV CCCCCCHHHCCCCCC	45.49	23927012
741	Phosphorylation	KESDLRRSEVPCAPM CHHHCCCCCCCCCCC	36.19	28555341
745	Glutathionylation	LRRSEVPCAPMPKKT CCCCCCCCCCCCCCC	8.85	22555962
748	Sulfoxidation	SEVPCAPMPKKTHQP CCCCCCCCCCCCCCC	3.96	21406390
756	Phosphorylation	PKKTHQPSDEVGTSI CCCCCCCCCCCCCCC	39.57	29214152
761	Phosphorylation	QPSDEVGTSIEHPRE CCCCCCCCCCCCHHH	31.54	28555341
762	Phosphorylation	PSDEVGTSIEHPREA CCCCCCCCCCCHHHH	21.76	25159151
773	Sulfoxidation	PREAEEVMDAGCQES HHHHHHHHHCCCCCC	3.10	21406390
792	Phosphorylation	RITDQEASENHVAAT CCCCHHHHHCCCCCC	37.87	28555341
808	Phosphorylation	SHLCVLRSRKLLKQL HHHHHHCHHHHHHHH	29.61	24719451
862	Phosphorylation	ALVWVSLSLLSKGSP HHHHHHHHHHCCCCC	21.54	24719451
927	Phosphorylation	RQKPGRASSDGPAGE CCCCCCCCCCCCCCC	27.83	20068231
928	Phosphorylation	QKPGRASSDGPAGEE CCCCCCCCCCCCCCC	45.67	26657352
944	Phosphorylation	VAGQEALTLGLWSGP CCCCHHEEECCCCCC	26.31	20068231
949	Phosphorylation	ALTLGLWSGPLPRVT HEEECCCCCCCCCEE	35.26	23090842
1015	Phosphorylation	RPPASLQYRFARIAI CCCHHHHHEEEEEEE	17.00	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of POP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of POP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of POP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPP29_HUMAN	POP4	physical	15096576
RPP38_HUMAN	RPP38	physical	15096576
RPP40_HUMAN	RPP40	physical	15096576
POP1_HUMAN	POP1	physical	15096576
NEDD8_HUMAN	NEDD8	physical	22863883
CSK22_HUMAN	CSNK2A2	physical	24778252
DICER_HUMAN	DICER1	physical	24778252
ELOC_HUMAN	TCEB1	physical	24778252
H10_HUMAN	H1F0	physical	24778252
IF6_HUMAN	EIF6	physical	24778252
MET17_HUMAN	METTL17	physical	24778252
MOV10_HUMAN	MOV10	physical	24778252
POP7_HUMAN	POP7	physical	24778252
PPM1G_HUMAN	PPM1G	physical	24778252
NOG1_HUMAN	GTPBP4	physical	24778252
CSK21_HUMAN	CSNK2A1	physical	24778252
EBP2_HUMAN	EBNA1BP2	physical	24778252
RENT1_HUMAN	UPF1	physical	24778252
RBM34_HUMAN	RBM34	physical	24778252
RPP29_HUMAN	POP4	physical	24778252
RPP30_HUMAN	RPP30	physical	24778252
RPP38_HUMAN	RPP38	physical	24778252
SIR1_HUMAN	SIRT1	physical	24778252
SORL_HUMAN	SORL1	physical	24778252
TRBP2_HUMAN	TARBP2	physical	24778252
ZN622_HUMAN	ZNF622	physical	24778252
G3BP1_HUMAN	G3BP1	physical	26344197
SF3A3_HUMAN	SF3A3	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-40 AND LYS-46, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-730, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-730, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-367 AND SER-730, ANDMASS SPECTROMETRY.
PubMed: 18669648

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, AND MASSSPECTROMETRY.
PubMed: 18187866

"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-371, AND MASSSPECTROMETRY.
PubMed: 19007248

"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 THR-365; SER-367; SER-371AND SER-584, AND MASS SPECTROMETRY.
PubMed: 17525332

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-730, ANDMASS SPECTROMETRY.
PubMed: 15302935

"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 THR-404, AND MASSSPECTROMETRY.
PubMed: 17924679