BOP1_HUMAN - dbPTM
BOP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BOP1_HUMAN
UniProt AC Q14137
Protein Name Ribosome biogenesis protein BOP1 {ECO:0000255|HAMAP-Rule:MF_03027}
Gene Name BOP1 {ECO:0000255|HAMAP-Rule:MF_03027}
Organism Homo sapiens (Human).
Sequence Length 746
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm .
Protein Description Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome..
Protein Sequence MAGSRGAGRTAAPSVRPEKRRSEPELEPEPEPEPPLLCTSPLSHSTGSDSGVSDSEESVFSGLEDSGSDSSEDDDEGDEEGEDGALDDEGHSGIKKTTEEQVQASTPCPRTEMASARIGDEYAEDSSDEEDIRNTVGNVPLEWYDDFPHVGYDLDGRRIYKPLRTRDELDQFLDKMDDPDYWRTVQDPMTGRDLRLTDEQVALVRRLQSGQFGDVGFNPYEPAVDFFSGDVMIHPVTNRPADKRSFIPSLVEKEKVSRMVHAIKMGWIQPRRPRDPTPSFYDLWAQEDPNAVLGRHKMHVPAPKLALPGHAESYNPPPEYLLSEEERLAWEQQEPGERKLSFLPRKFPSLRAVPAYGRFIQERFERCLDLYLCPRQRKMRVNVDPEDLIPKLPRPRDLQPFPTCQALVYRGHSDLVRCLSVSPGGQWLVSGSDDGSLRLWEVATARCVRTVPVGGVVKSVAWNPSPAVCLVAAAVEDSVLLLNPALGDRLVAGSTDQLLSAFVPPEEPPLQPARWLEASEEERQVGLRLRICHGKPVTQVTWHGRGDYLAVVLATQGHTQVLIHQLSRRRSQSPFRRSHGQVQRVAFHPARPFLLVASQRSVRLYHLLRQELTKKLMPNCKWVSSLAVHPAGDNVICGSYDSKLVWFDLDLSTKPYRMLRHHKKALRAVAFHPRYPLFASGSDDGSVIVCHGMVYNDLLQNPLLVPVKVLKGHVLTRDLGVLDVIFHPTQPWVFSSGADGTVRLFT
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 Orthologous
Protein Cluster
2Acetylation------MAGSRGAGR
------CCCCCCCCC		25.35-
5Methylation---MAGSRGAGRTAA
---CCCCCCCCCCCC		37.75-
9MethylationAGSRGAGRTAAPSVR
CCCCCCCCCCCCCCC		22.21-
14PhosphorylationAGRTAAPSVRPEKRR
CCCCCCCCCCCCCCC		26.4928555341
19AcetylationAPSVRPEKRRSEPEL
CCCCCCCCCCCCCCC		56.6523749302
19UbiquitinationAPSVRPEKRRSEPEL
CCCCCCCCCCCCCCC		56.6524816145
40PhosphorylationEPPLLCTSPLSHSTG
CCCEEECCCCCCCCC		23.89-
96UbiquitinationEGHSGIKKTTEEQVQ
CCCCCCCCCHHHHHH		59.7733845483
97PhosphorylationGHSGIKKTTEEQVQA
CCCCCCCCHHHHHHH		34.1424732914
98PhosphorylationHSGIKKTTEEQVQAS
CCCCCCCHHHHHHHC		46.5424732914
105PhosphorylationTEEQVQASTPCPRTE
HHHHHHHCCCCCCHH		18.7829255136
106PhosphorylationEEQVQASTPCPRTEM
HHHHHHCCCCCCHHH		31.7429255136
108GlutathionylationQVQASTPCPRTEMAS
HHHHCCCCCCHHHHH		3.4522555962
108S-nitrosylationQVQASTPCPRTEMAS
HHHHCCCCCCHHHHH		3.452212679
122PhosphorylationSARIGDEYAEDSSDE
HHHCCHHHCCCCCCH		21.7422167270
126PhosphorylationGDEYAEDSSDEEDIR
CHHHCCCCCCHHHHH		31.0629255136
127PhosphorylationDEYAEDSSDEEDIRN
HHHCCCCCCHHHHHH		62.4529255136
135PhosphorylationDEEDIRNTVGNVPLE
CHHHHHHHCCCCCCE		21.6823898821
144PhosphorylationGNVPLEWYDDFPHVG
CCCCCEECCCCCCCE		9.0328464451
152PhosphorylationDDFPHVGYDLDGRRI
CCCCCCEECCCCCEE		16.5521406692
161AcetylationLDGRRIYKPLRTRDE
CCCCEECCCCCCHHH		34.8926051181
161UbiquitinationLDGRRIYKPLRTRDE
CCCCEECCCCCCHHH		34.89-
175UbiquitinationELDQFLDKMDDPDYW
HHHHHHHHCCCCCHH		46.5021906983
181PhosphorylationDKMDDPDYWRTVQDP
HHCCCCCHHCCCCCC		11.3727642862
197PhosphorylationTGRDLRLTDEQVALV
CCCCCCCCHHHHHHH		30.9321712546
209PhosphorylationALVRRLQSGQFGDVG
HHHHHHHCCCCCCCC		38.8727642862
220PhosphorylationGDVGFNPYEPAVDFF
CCCCCCCCCCCCCCC		35.3320068231
228PhosphorylationEPAVDFFSGDVMIHP
CCCCCCCCCCEEEEE		33.7920068231
237PhosphorylationDVMIHPVTNRPADKR
CEEEEECCCCCCCHH		29.9320068231
245PhosphorylationNRPADKRSFIPSLVE
CCCCCHHCCCHHHHH		33.0128555341
249PhosphorylationDKRSFIPSLVEKEKV
CHHCCCHHHHHHHHH		39.9828555341
253UbiquitinationFIPSLVEKEKVSRMV
CCHHHHHHHHHHHHH		56.1921906983
253UbiquitinationFIPSLVEKEKVSRMV
CCHHHHHHHHHHHHH		56.1921890473
255UbiquitinationPSLVEKEKVSRMVHA
HHHHHHHHHHHHHHH		57.4922817900
264UbiquitinationSRMVHAIKMGWIQPR
HHHHHHHHCCCCCCC		31.95-
277PhosphorylationPRRPRDPTPSFYDLW
CCCCCCCCCCHHHHH		35.5322817900
279PhosphorylationRPRDPTPSFYDLWAQ
CCCCCCCCHHHHHCC		38.6328348404
297UbiquitinationNAVLGRHKMHVPAPK
CCCCCCCCCCCCCCC		29.3729967540
304UbiquitinationKMHVPAPKLALPGHA
CCCCCCCCCCCCCCH		48.8022817900
320PhosphorylationSYNPPPEYLLSEEER
HCCCCHHHHCCHHHH		20.7929978859
323PhosphorylationPPPEYLLSEEERLAW
CCHHHHCCHHHHHHH		40.1321815630
339UbiquitinationQQEPGERKLSFLPRK
HCCCCCCCCCCCCCC		44.1533845483
339AcetylationQQEPGERKLSFLPRK
HCCCCCCCCCCCCCC		44.1519824901
341PhosphorylationEPGERKLSFLPRKFP
CCCCCCCCCCCCCCC		27.9826462736
349PhosphorylationFLPRKFPSLRAVPAY
CCCCCCCCCCCCCCH		33.3526434776
371PhosphorylationFERCLDLYLCPRQRK
HHHHHHHHCCCCCCC		13.11-
391AcetylationDPEDLIPKLPRPRDL
CHHHHCCCCCCCCCC		65.2226051181
391UbiquitinationDPEDLIPKLPRPRDL
CHHHHCCCCCCCCCC		65.2221906983
391UbiquitinationDPEDLIPKLPRPRDL
CHHHHCCCCCCCCCC		65.2221890473
410MethylationTCQALVYRGHSDLVR
CCCEEEECCCCCCEE		28.95-
413PhosphorylationALVYRGHSDLVRCLS
EEEECCCCCCEEEEE		35.1522210691
420PhosphorylationSDLVRCLSVSPGGQW
CCCEEEEEECCCCCE		24.9527251275
422PhosphorylationLVRCLSVSPGGQWLV
CEEEEEECCCCCEEE		17.9122210691
430PhosphorylationPGGQWLVSGSDDGSL
CCCCEEEECCCCCCE		30.3422210691
432PhosphorylationGQWLVSGSDDGSLRL
CCEEEECCCCCCEEE		25.6427251275
436PhosphorylationVSGSDDGSLRLWEVA
EECCCCCCEEEEEEE		19.8127251275
444PhosphorylationLRLWEVATARCVRTV
EEEEEEEEEEEEEEE		21.5827251275
535AcetylationRLRICHGKPVTQVTW
EEEEECCCCCEEEEE		16.7926051181
573PhosphorylationLSRRRSQSPFRRSHG
HHHCCCCCCCCCCCC		27.5324719451
598PhosphorylationRPFLLVASQRSVRLY
CCEEEEECHHHHHHH		20.7429523821
614UbiquitinationLLRQELTKKLMPNCK
HHHHHHHHHHCCCCE		57.4427667366
615UbiquitinationLRQELTKKLMPNCKW
HHHHHHHHHCCCCEE		44.79-
621AcetylationKKLMPNCKWVSSLAV
HHHCCCCEEEEEEEE		58.2226051181
621UbiquitinationKKLMPNCKWVSSLAV
HHHCCCCEEEEEEEE		58.22-
640PhosphorylationDNVICGSYDSKLVWF
CCEEEEECCCEEEEE		14.98-
642PhosphorylationVICGSYDSKLVWFDL
EEEEECCCEEEEEEE		21.47-
654UbiquitinationFDLDLSTKPYRMLRH
EEECCCCHHHHHHHH		36.3521906983
711UbiquitinationLVPVKVLKGHVLTRD
EEEHEEECCCEEECC		50.3829967540
711MethylationLVPVKVLKGHVLTRD
EEEHEEECCCEEECC		50.38-
716PhosphorylationVLKGHVLTRDLGVLD
EECCCEEECCCCCEE		22.5024043423
729PhosphorylationLDVIFHPTQPWVFSS
EEEEECCCCCCEEEC		38.4024043423
735PhosphorylationPTQPWVFSSGADGTV
CCCCCEEECCCCCEE		20.4524043423
736PhosphorylationTQPWVFSSGADGTVR
CCCCEEECCCCCEEE		26.9124043423
741PhosphorylationFSSGADGTVRLFT--
EECCCCCEEEECC--		11.7324043423
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 BOP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BOP1_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 BOP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR12_HUMANWDR12physical
16738141
PESC_HUMANPES1physical
16738141
PESC_HUMANPES1physical
17353269
WDR12_HUMANWDR12physical
17353269
NOP58_HUMANNOP58physical
22939629
FBRL_HUMANFBLphysical
22939629
NOP2_HUMANNOP2physical
22939629
NOP56_HUMANNOP56physical
22939629
RS7_HUMANRPS7physical
22939629
NH2L1_HUMANNHP2L1physical
22939629
RL30_HUMANRPL30physical
22939629
GNL3_HUMANGNL3physical
22939629
PESC_HUMANPES1physical
16043514
BOP1_HUMANBOP1physical
16043514
WDR12_HUMANWDR12physical
16043514
MAOX_HUMANME1physical
22863883
SNX5_HUMANSNX5physical
22863883
UGDH_HUMANUGDHphysical
22863883
WDR12_HUMANWDR12physical
26601951
MDN1_HUMANMDN1physical
26601951
PESC_HUMANPES1physical
26601951
DDX27_HUMANDDX27physical
25825154
PESC_HUMANPES1physical
25825154
HIP1R_HUMANHIP1Rphysical
25825154
WDR74_HUMANWDR74physical
25825154
BUB3_HUMANBUB3physical
25825154
MYH9_HUMANMYH9physical
25825154
OTUL_HUMANOTULINphysical
25825154
RL7L_HUMANRPL7L1physical
25825154
NDUF3_HUMANNDUFAF3physical
25825154
WDR12_HUMANWDR12physical
25825154
ACAP1_HUMANACAP1physical
25825154
SYT10_HUMANSYT10physical
25825154
CHAP1_HUMANCHAMP1physical
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 BOP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-106; SER-126 AND SER-127, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-126 AND SER-127, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-106; SER-126 AND SER-127, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, ANDMASS SPECTROMETRY.
"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 THR-106; SER-126; SER-127AND THR-197, AND MASS SPECTROMETRY.
"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-126 AND SER-127, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, ANDMASS SPECTROMETRY.
"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-126 AND SER-127, ANDMASS SPECTROMETRY.
"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 THR-106, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, AND MASSSPECTROMETRY.
"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 THR-106, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory