RN169_HUMAN - dbPTM
RN169_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN169_HUMAN
UniProt AC Q8NCN4
Protein Name E3 ubiquitin-protein ligase RNF169
Gene Name RNF169
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Nucleus, nucleoplasm . Localizes to sites of double-strand breaks (DSBs) following DNA damage. Recruited to DSBs via recognition of RNF168-dependent ubiquitin products.
Protein Description Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair..
Protein Sequence MAAAGPSTRASSAAAAAALSRRGRRGRCDETAAAKTGAPGPASGPSLLVLSPPLLQPPLPPRPEESGCAGCLEPPGEAAALPCGHSLCRGCAQRAADAAGPGCPRCRARGPGWARRRARDDGQADSEVLGECARRSQPERCRPRRDGGAAAAGPRPEQEPRAAPAEPDFIFRAPIKLSKPGELREEYESLRKLREEKLQEEKPSEDQIHKLLPEDTETGKRKMDEQKKRDEPLVLKTNLERCPARLSDSENEEPSRGQMTQTHRSAFVSKNNSYSLAFLAGKLNSKVERSQSCSDTAQERAKSRVRAVPGNKAKVTTMTPASNPIIGVLLSTQNNRCVSAPDLTIEKRLPFSSLSSLASLHKPERSVSPESNDSISEELNHFKPIVCSPCTPPKRLPDGRVLSPLIIKSTPRNLNRSLQKQTSYEASPRILKKWEQIFQERQIKKTLSKATLTSLAPEMGEELLGSEGIHSSKEKPLVAVNTRLSGGQVLSEYTGPTSADLDHFPSVSQTKAEQDSDNKSSTEIPLETCCSSELKGGGSGTSLEREQFEGLGSTPDAKLDKTCISRAMKITTVNSVLPQNSVLGGVLKTKQQLKTLNHFDLTNGVLVESLSEEPLPSLRRGRKRHCKTKHLEQNGSLKKLRQTSGEVGLAPTDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRTVSRRKGSVDQYLLRSSNMAGAK
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
7Phosphorylation-MAAAGPSTRASSAA
-CCCCCCCHHHHHHH		29.6120068231
8PhosphorylationMAAAGPSTRASSAAA
CCCCCCCHHHHHHHH		33.1320068231
9MethylationAAAGPSTRASSAAAA
CCCCCCHHHHHHHHH		36.49115491401
11PhosphorylationAGPSTRASSAAAAAA
CCCCHHHHHHHHHHH		19.7428122231
12PhosphorylationGPSTRASSAAAAAAL
CCCHHHHHHHHHHHH		22.4223401153
20PhosphorylationAAAAAALSRRGRRGR
HHHHHHHHHCCCCCC		18.4020068231
176AcetylationFIFRAPIKLSKPGEL
CEEECCCCCCCCCHH		45.7225953088
187PhosphorylationPGELREEYESLRKLR
CCHHHHHHHHHHHHH		13.1828796482
236UbiquitinationRDEPLVLKTNLERCP
HCCCCCHHHCHHHCC		28.0829967540
247PhosphorylationERCPARLSDSENEEP
HHCCCCCCCCCCCCC		33.2723401153
249PhosphorylationCPARLSDSENEEPSR
CCCCCCCCCCCCCCC		38.6623401153
255PhosphorylationDSENEEPSRGQMTQT
CCCCCCCCCCCCCCH		52.9323927012
260PhosphorylationEPSRGQMTQTHRSAF
CCCCCCCCCHHHHHH		23.5627174698
262PhosphorylationSRGQMTQTHRSAFVS
CCCCCCCHHHHHHCC		15.3027174698
270SumoylationHRSAFVSKNNSYSLA
HHHHHCCCCCCHHHH		55.64-
270SumoylationHRSAFVSKNNSYSLA
HHHHHCCCCCCHHHH		55.64-
273PhosphorylationAFVSKNNSYSLAFLA
HHCCCCCCHHHHHHH		26.0325159151
274PhosphorylationFVSKNNSYSLAFLAG
HCCCCCCHHHHHHHH		15.1625627689
275PhosphorylationVSKNNSYSLAFLAGK
CCCCCCHHHHHHHHH		17.0328555341
282AcetylationSLAFLAGKLNSKVER
HHHHHHHHHCHHHHH		38.6026051181
282UbiquitinationSLAFLAGKLNSKVER
HHHHHHHHHCHHHHH		38.6021890473
286SumoylationLAGKLNSKVERSQSC
HHHHHCHHHHHHHCC		47.22-
286SumoylationLAGKLNSKVERSQSC
HHHHHCHHHHHHHCC		47.2228112733
290PhosphorylationLNSKVERSQSCSDTA
HCHHHHHHHCCCHHH		16.9725159151
292PhosphorylationSKVERSQSCSDTAQE
HHHHHHHCCCHHHHH		19.4825159151
294PhosphorylationVERSQSCSDTAQERA
HHHHHCCCHHHHHHH		43.1530242111
296PhosphorylationRSQSCSDTAQERAKS
HHHCCCHHHHHHHHH		17.5926552605
303UbiquitinationTAQERAKSRVRAVPG
HHHHHHHHHHEECCC		34.7221890473
316PhosphorylationPGNKAKVTTMTPASN
CCCCCEEEEECCCCC		15.3328122231
317PhosphorylationGNKAKVTTMTPASNP
CCCCEEEEECCCCCC		23.2628348404
319PhosphorylationKAKVTTMTPASNPII
CCEEEEECCCCCCEE		17.3828348404
322PhosphorylationVTTMTPASNPIIGVL
EEEECCCCCCEEEEE		44.3221815630
331PhosphorylationPIIGVLLSTQNNRCV
CEEEEEEECCCCEEE		24.6429514088
332PhosphorylationIIGVLLSTQNNRCVS
EEEEEEECCCCEEEC		34.9729514088
339PhosphorylationTQNNRCVSAPDLTIE
CCCCEEECCCCCEEE		37.4023401153
344PhosphorylationCVSAPDLTIEKRLPF
EECCCCCEEEECCCC		34.1723403867
347UbiquitinationAPDLTIEKRLPFSSL
CCCCEEEECCCCCHH		56.2229967540
353PhosphorylationEKRLPFSSLSSLASL
EECCCCCHHHHHHHC		32.4228555341
356PhosphorylationLPFSSLSSLASLHKP
CCCCHHHHHHHCCCC		32.9928555341
359PhosphorylationSSLSSLASLHKPERS
CHHHHHHHCCCCCCC		35.9826074081
362AcetylationSSLASLHKPERSVSP
HHHHHCCCCCCCCCC		54.5926051181
362SumoylationSSLASLHKPERSVSP
HHHHHCCCCCCCCCC		54.5928112733
362UbiquitinationSSLASLHKPERSVSP
HHHHHCCCCCCCCCC		54.5929967540
366PhosphorylationSLHKPERSVSPESND
HCCCCCCCCCCCCCC		25.8622617229
368PhosphorylationHKPERSVSPESNDSI
CCCCCCCCCCCCCCH		24.9723401153
371PhosphorylationERSVSPESNDSISEE
CCCCCCCCCCCHHHH		49.6927362937
374PhosphorylationVSPESNDSISEELNH
CCCCCCCCHHHHHHC		32.0627362937
376PhosphorylationPESNDSISEELNHFK
CCCCCCHHHHHHCCC		29.0419276368
388PhosphorylationHFKPIVCSPCTPPKR
CCCCCEECCCCCCCC		16.4725159151
391PhosphorylationPIVCSPCTPPKRLPD
CCEECCCCCCCCCCC		46.1123401153
403PhosphorylationLPDGRVLSPLIIKST
CCCCCEECCEEECCC		18.1429255136
408SumoylationVLSPLIIKSTPRNLN
EECCEEECCCCCCHH		41.08-
408SumoylationVLSPLIIKSTPRNLN
EECCEEECCCCCCHH		41.08-
408UbiquitinationVLSPLIIKSTPRNLN
EECCEEECCCCCCHH		41.0829967540
409PhosphorylationLSPLIIKSTPRNLNR
ECCEEECCCCCCHHH		32.9825159151
410PhosphorylationSPLIIKSTPRNLNRS
CCEEECCCCCCHHHH		22.6725159151
417PhosphorylationTPRNLNRSLQKQTSY
CCCCHHHHHHHHCCC		33.7920068231
420MethylationNLNRSLQKQTSYEAS
CHHHHHHHHCCCCCC		61.92115976785
420UbiquitinationNLNRSLQKQTSYEAS
CHHHHHHHHCCCCCC		61.9229967540
422PhosphorylationNRSLQKQTSYEASPR
HHHHHHHCCCCCCHH		40.0728450419
423PhosphorylationRSLQKQTSYEASPRI
HHHHHHCCCCCCHHH		20.6225159151
424PhosphorylationSLQKQTSYEASPRIL
HHHHHCCCCCCHHHH		20.9230576142
427PhosphorylationKQTSYEASPRILKKW
HHCCCCCCHHHHHHH		11.6325159151
433SumoylationASPRILKKWEQIFQE
CCHHHHHHHHHHHHH		53.14-
433SumoylationASPRILKKWEQIFQE
CCHHHHHHHHHHHHH		53.14-
433UbiquitinationASPRILKKWEQIFQE
CCHHHHHHHHHHHHH		53.1429967540
449UbiquitinationQIKKTLSKATLTSLA
HHHHHHCHHHHHHHC		48.8029967540
451PhosphorylationKKTLSKATLTSLAPE
HHHHCHHHHHHHCHH		34.0128555341
453PhosphorylationTLSKATLTSLAPEMG
HHCHHHHHHHCHHHH		19.8322210691
466PhosphorylationMGEELLGSEGIHSSK
HHHHHHCCCCCCCCC		32.4022210691
471PhosphorylationLGSEGIHSSKEKPLV
HCCCCCCCCCCCCEE		40.9820068231
472PhosphorylationGSEGIHSSKEKPLVA
CCCCCCCCCCCCEEE		30.5825627689
473UbiquitinationSEGIHSSKEKPLVAV
CCCCCCCCCCCEEEE		73.1629967540
475SumoylationGIHSSKEKPLVAVNT
CCCCCCCCCEEEEEE		47.60-
475SumoylationGIHSSKEKPLVAVNT
CCCCCCCCCEEEEEE		47.60-
475UbiquitinationGIHSSKEKPLVAVNT
CCCCCCCCCEEEEEE		47.6029967540
482PhosphorylationKPLVAVNTRLSGGQV
CCEEEEEEECCCCCE		26.7925627689
485PhosphorylationVAVNTRLSGGQVLSE
EEEEEECCCCCEECC		37.2725159151
491PhosphorylationLSGGQVLSEYTGPTS
CCCCCEECCCCCCCC		29.6927732954
493PhosphorylationGGQVLSEYTGPTSAD
CCCEECCCCCCCCCC		17.3927251275
494PhosphorylationGQVLSEYTGPTSADL
CCEECCCCCCCCCCC		32.4127251275
497PhosphorylationLSEYTGPTSADLDHF
ECCCCCCCCCCCCCC		37.5827251275
498PhosphorylationSEYTGPTSADLDHFP
CCCCCCCCCCCCCCC		23.9526714015
506PhosphorylationADLDHFPSVSQTKAE
CCCCCCCCHHHCCCC		33.1923186163
508PhosphorylationLDHFPSVSQTKAEQD
CCCCCCHHHCCCCCC		36.1530576142
510PhosphorylationHFPSVSQTKAEQDSD
CCCCHHHCCCCCCCC		25.3930576142
511SumoylationFPSVSQTKAEQDSDN
CCCHHHCCCCCCCCC		42.1428112733
511UbiquitinationFPSVSQTKAEQDSDN
CCCHHHCCCCCCCCC		42.1429967540
516PhosphorylationQTKAEQDSDNKSSTE
HCCCCCCCCCCCCCC		42.6623401153
520PhosphorylationEQDSDNKSSTEIPLE
CCCCCCCCCCCCCHH		49.0730576142
521PhosphorylationQDSDNKSSTEIPLET
CCCCCCCCCCCCHHH		31.5025159151
522PhosphorylationDSDNKSSTEIPLETC
CCCCCCCCCCCHHHH		45.0525159151
528PhosphorylationSTEIPLETCCSSELK
CCCCCHHHHHCCCCC		26.8828450419
531PhosphorylationIPLETCCSSELKGGG
CCHHHHHCCCCCCCC		29.0626657352
532PhosphorylationPLETCCSSELKGGGS
CHHHHHCCCCCCCCC		32.7921815630
535UbiquitinationTCCSSELKGGGSGTS
HHHCCCCCCCCCCCC		52.0029967540
539PhosphorylationSELKGGGSGTSLERE
CCCCCCCCCCCCCHH		42.0230576142
541PhosphorylationLKGGGSGTSLEREQF
CCCCCCCCCCCHHHH		31.6625159151
542PhosphorylationKGGGSGTSLEREQFE
CCCCCCCCCCHHHHC		31.5825159151
553PhosphorylationEQFEGLGSTPDAKLD
HHHCCCCCCCCHHCC		41.6423401153
554PhosphorylationQFEGLGSTPDAKLDK
HHCCCCCCCCHHCCH		24.3223401153
558UbiquitinationLGSTPDAKLDKTCIS
CCCCCCHHCCHHHHH		65.6832015554
561AcetylationTPDAKLDKTCISRAM
CCCHHCCHHHHHHHH		56.597709767
561UbiquitinationTPDAKLDKTCISRAM
CCCHHCCHHHHHHHH		56.5929967540
569UbiquitinationTCISRAMKITTVNSV
HHHHHHHCHHCCCCC		35.60-
588SumoylationSVLGGVLKTKQQLKT
CHHHHHHCHHHHHHH		51.80-
588SumoylationSVLGGVLKTKQQLKT
CHHHHHHCHHHHHHH		51.80-
590UbiquitinationLGGVLKTKQQLKTLN
HHHHHCHHHHHHHCC		34.16-
617PhosphorylationLSEEPLPSLRRGRKR
CCCCCCHHHHCCCHH		42.0424719451
629UbiquitinationRKRHCKTKHLEQNGS
CHHHHCCHHHHHCCC		31.5229967540
636PhosphorylationKHLEQNGSLKKLRQT
HHHHHCCCHHHHHHC		44.5625159151
638SumoylationLEQNGSLKKLRQTSG
HHHCCCHHHHHHCCC		52.00-
638SumoylationLEQNGSLKKLRQTSG
HHHCCCHHHHHHCCC		52.00-
638UbiquitinationLEQNGSLKKLRQTSG
HHHCCCHHHHHHCCC		52.0029967540
639SumoylationEQNGSLKKLRQTSGE
HHCCCHHHHHHCCCC		54.95-
639SumoylationEQNGSLKKLRQTSGE
HHCCCHHHHHHCCCC		54.95-
643PhosphorylationSLKKLRQTSGEVGLA
CHHHHHHCCCCCCCC		32.0630108239
644PhosphorylationLKKLRQTSGEVGLAP
HHHHHHCCCCCCCCC		25.3125159151
652PhosphorylationGEVGLAPTDPVLREM
CCCCCCCCCHHHHHH		47.53-
688PhosphorylationDNERRTVSRRKGSVD
HCCCCHHHHCCCCHH		26.25-
691UbiquitinationRRTVSRRKGSVDQYL
CCHHHHCCCCHHHHH		55.2021963094
693PhosphorylationTVSRRKGSVDQYLLR
HHHHCCCCHHHHHHH		26.0925159151
697PhosphorylationRKGSVDQYLLRSSNM
CCCCHHHHHHHHCCC		11.8423312004
701PhosphorylationVDQYLLRSSNMAGAK
HHHHHHHHCCCCCCC		26.4917081983
702PhosphorylationDQYLLRSSNMAGAK-
HHHHHHHCCCCCCC-		24.9617081983
712UbiquitinationAGAK-----------
CCCC-----------		21963094
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 RN169_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN169_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 RN169_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
22742833
H2A2C_HUMANHIST2H2ACphysical
22742833
H2B2E_HUMANHIST2H2BEphysical
22742833
UB2E1_HUMANUBE2E1physical
22492721
UBP7_HUMANUSP7physical
28325877
DYR1A_HUMANDYRK1Aphysical
28325877
DYR1B_HUMANDYRK1Bphysical
28325877
CAPZB_HUMANCAPZBphysical
28325877
DCAF7_HUMANDCAF7physical
28325877
CAZA1_HUMANCAPZA1physical
28325877
TBB4B_HUMANTUBB4Bphysical
28325877
RS3_HUMANRPS3physical
28325877
DDB1_HUMANDDB1physical
28325877
C1QBP_HUMANC1QBPphysical
28325877
HNRPU_HUMANHNRNPUphysical
28325877
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 RN169_HUMAN

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Related Literatures of Post-Translational Modification
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-403 AND THR-554, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-391 AND SER-403, 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 SER-247; SER-249; SER-403;SER-409; THR-410; THR-554 AND SER-693, 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-403; SER-485 ANDTHR-554, AND MASS 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 SER-247, 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 SER-403, AND MASSSPECTROMETRY.
"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-339, AND MASSSPECTROMETRY.
"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-292 AND SER-427, ANDMASS SPECTROMETRY.

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