RN168_HUMAN - dbPTM
RN168_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN168_HUMAN
UniProt AC Q8IYW5
Protein Name E3 ubiquitin-protein ligase RNF168 {ECO:0000255|HAMAP-Rule:MF_03066}
Gene Name RNF168 {ECO:0000255|HAMAP-Rule:MF_03066}
Organism Homo sapiens (Human).
Sequence Length 571
Subcellular Localization Nucleus . Localizes to double-strand breaks (DSBs) sites of DNA damage.
Protein Description E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively)..
Protein Sequence MALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLCCPFCRRRVSSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLLSKPGELRREYEEEISKVAAERRASEEEENKASEEYIQRLLAEEEEEEKRQAEKRRRAMEEQLKSDEELARKLSIDINNFCEGSISASPLNSRKSDPVTPKSEKKSKNKQRNTGDIQKYLTPKSQFGSASHSEAVQEVRKDSVSKDIDSSDRKSPTGQDTEIEDMPTLSPQISLGVGEQGADSSIESPMPWLCACGAEWYHEGNVKTRPSNHGKELCVLSHERPKTRVPYSKETAVMPCGRTESGCAPTSGVTQTNGNNTGETENEESCLLISKEISKRKNQESSFEAVKDPCFSAKRRKVSPESSPDQEETEINFTQKLIDLEHLLFERHKQEEQDRLLALQLQKEVDKEQMVPNRQKGSPDEYHLRATSSPPDKVLNGQRKNPKDGNFKRQTHTKHPTPERGSRDKNRQVSLKMQLKQSVNRRKMPNSTRDHCKVSKSAHSLQPSISQKSVFQMFQRCTK
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
59PhosphorylationPFCRRRVSSWTRYHT
HHHHHHHHHHHHHHH		20.5322617229
62PhosphorylationRRRVSSWTRYHTRRN
HHHHHHHHHHHHCCC		24.2522617229
70PhosphorylationRYHTRRNSLVNVELW
HHHHCCCCEECHHHH		31.7028450419
93PhosphorylationRECKLRASGQESEEV
CCCCCCCCCCCCHHH		34.2822210691
104PhosphorylationSEEVADDYQPVRLLS
CHHHHHCCCCEEHHC		18.4428796482
111PhosphorylationYQPVRLLSKPGELRR
CCCEEHHCCCCHHHH		41.2028555341
112UbiquitinationQPVRLLSKPGELRRE
CCEEHHCCCCHHHHH		57.9429967540
126UbiquitinationEYEEEISKVAAERRA
HHHHHHHHHHHHHHC		41.3732015554
134PhosphorylationVAAERRASEEEENKA
HHHHHHCCHHHHHHH		43.6723401153
140UbiquitinationASEEEENKASEEYIQ
CCHHHHHHHCHHHHH		57.4829967540
142PhosphorylationEEEENKASEEYIQRL
HHHHHHHCHHHHHHH		32.3523186163
158UbiquitinationAEEEEEEKRQAEKRR
HHHHHHHHHHHHHHH		53.7624816145
173UbiquitinationRAMEEQLKSDEELAR
HHHHHHHHCHHHHHH		56.40-
174PhosphorylationAMEEQLKSDEELARK
HHHHHHHCHHHHHHH		59.8723401153
181UbiquitinationSDEELARKLSIDINN
CHHHHHHHHCCCCCC		40.7629967540
183PhosphorylationEELARKLSIDINNFC
HHHHHHHCCCCCCCC		22.6526074081
193PhosphorylationINNFCEGSISASPLN
CCCCCCCCCCCCCCC		7.3526074081
195PhosphorylationNFCEGSISASPLNSR
CCCCCCCCCCCCCCC		25.1326074081
197PhosphorylationCEGSISASPLNSRKS
CCCCCCCCCCCCCCC		24.1125159151
201PhosphorylationISASPLNSRKSDPVT
CCCCCCCCCCCCCCC		49.0926074081
203UbiquitinationASPLNSRKSDPVTPK
CCCCCCCCCCCCCCC		60.0627667366
204PhosphorylationSPLNSRKSDPVTPKS
CCCCCCCCCCCCCCC		46.1427794612
208PhosphorylationSRKSDPVTPKSEKKS
CCCCCCCCCCCHHCC		30.3230576142
210UbiquitinationKSDPVTPKSEKKSKN
CCCCCCCCCHHCCCC		62.9829967540
210SumoylationKSDPVTPKSEKKSKN
CCCCCCCCCHHCCCC		62.9828112733
210SumoylationKSDPVTPKSEKKSKN
CCCCCCCCCHHCCCC		62.98-
211PhosphorylationSDPVTPKSEKKSKNK
CCCCCCCCHHCCCCC		56.7130576142
218UbiquitinationSEKKSKNKQRNTGDI
CHHCCCCCCCCCCCH		55.1329967540
227UbiquitinationRNTGDIQKYLTPKSQ
CCCCCHHHHCCCHHH		42.4323000965
230PhosphorylationGDIQKYLTPKSQFGS
CCHHHHCCCHHHCCC		26.11-
232UbiquitinationIQKYLTPKSQFGSAS
HHHHCCCHHHCCCCC		52.2123000965
237PhosphorylationTPKSQFGSASHSEAV
CCHHHCCCCCHHHHH		28.0825159151
239PhosphorylationKSQFGSASHSEAVQE
HHHCCCCCHHHHHHH		29.2827134283
249UbiquitinationEAVQEVRKDSVSKDI
HHHHHHHHHHCCCCC		60.5829967540
251PhosphorylationVQEVRKDSVSKDIDS
HHHHHHHHCCCCCCC		31.1823882029
253PhosphorylationEVRKDSVSKDIDSSD
HHHHHHCCCCCCCCC		28.6723882029
254UbiquitinationVRKDSVSKDIDSSDR
HHHHHCCCCCCCCCC		57.4529967540
278PhosphorylationIEDMPTLSPQISLGV
CCCCCCCCCCEEECC		19.7626074081
323UbiquitinationTRPSNHGKELCVLSH
CCCCCCCCEEEEEEC		39.7129967540
329PhosphorylationGKELCVLSHERPKTR
CCEEEEEECCCCCCC		11.69-
334UbiquitinationVLSHERPKTRVPYSK
EEECCCCCCCCCCCC		56.0029967540
341UbiquitinationKTRVPYSKETAVMPC
CCCCCCCCCEEEEEC		53.9223000965
362PhosphorylationCAPTSGVTQTNGNNT
CCCCCCCCCCCCCCC		32.95-
383UbiquitinationESCLLISKEISKRKN
HHEEEEHHHHHHHCC		52.6621963094
387UbiquitinationLISKEISKRKNQESS
EEHHHHHHHCCCCCH		73.4022817900
389UbiquitinationSKEISKRKNQESSFE
HHHHHHHCCCCCHHH		67.7229967540
393PhosphorylationSKRKNQESSFEAVKD
HHHCCCCCHHHHHCC		30.4825159151
394PhosphorylationKRKNQESSFEAVKDP
HHCCCCCHHHHHCCH		26.7625849741
399UbiquitinationESSFEAVKDPCFSAK
CCHHHHHCCHHHCCC		64.1022505724
404PhosphorylationAVKDPCFSAKRRKVS
HHCCHHHCCCCCCCC		39.33-
406UbiquitinationKDPCFSAKRRKVSPE
CCHHHCCCCCCCCCC		52.0822817900
409UbiquitinationCFSAKRRKVSPESSP
HHCCCCCCCCCCCCC		51.6121906983
411PhosphorylationSAKRRKVSPESSPDQ
CCCCCCCCCCCCCCH		26.4530266825
414PhosphorylationRRKVSPESSPDQEET
CCCCCCCCCCCHHHH		51.0230266825
415PhosphorylationRKVSPESSPDQEETE
CCCCCCCCCCHHHHH		30.7323401153
421PhosphorylationSSPDQEETEINFTQK
CCCCHHHHHCCHHHH		41.2222167270
426PhosphorylationEETEINFTQKLIDLE
HHHHCCHHHHHHHHH		21.9526074081
428UbiquitinationTEINFTQKLIDLEHL
HHCCHHHHHHHHHHH		44.3329967540
441UbiquitinationHLLFERHKQEEQDRL
HHHHHHHHHHHHHHH		66.6729967540
455UbiquitinationLLALQLQKEVDKEQM
HHHHHHHHHCCHHHC		69.1921906983
459UbiquitinationQLQKEVDKEQMVPNR
HHHHHCCHHHCCCCC		55.8322817900
468UbiquitinationQMVPNRQKGSPDEYH
HCCCCCCCCCCCCCC		59.1127667366
468SumoylationQMVPNRQKGSPDEYH
HCCCCCCCCCCCCCC		59.11-
468SumoylationQMVPNRQKGSPDEYH
HCCCCCCCCCCCCCC		59.11-
470PhosphorylationVPNRQKGSPDEYHLR
CCCCCCCCCCCCCCC		35.8925159151
474PhosphorylationQKGSPDEYHLRATSS
CCCCCCCCCCCCCCC		17.3423186163
479PhosphorylationDEYHLRATSSPPDKV
CCCCCCCCCCCCHHH		24.2530266825
480PhosphorylationEYHLRATSSPPDKVL
CCCCCCCCCCCHHHH		39.6030266825
481PhosphorylationYHLRATSSPPDKVLN
CCCCCCCCCCHHHHC		35.7830266825
485UbiquitinationATSSPPDKVLNGQRK
CCCCCCHHHHCCCCC		55.1627667366
492UbiquitinationKVLNGQRKNPKDGNF
HHHCCCCCCCCCCCC		70.4824816145
495UbiquitinationNGQRKNPKDGNFKRQ
CCCCCCCCCCCCCCC		83.8527667366
500UbiquitinationNPKDGNFKRQTHTKH
CCCCCCCCCCCCCCC		47.8229967540
506UbiquitinationFKRQTHTKHPTPERG
CCCCCCCCCCCCCCC		39.7329967540
509PhosphorylationQTHTKHPTPERGSRD
CCCCCCCCCCCCCCC		37.1826074081
524UbiquitinationKNRQVSLKMQLKQSV
CCCHHHHHHHHHHHH		19.6622817900
528UbiquitinationVSLKMQLKQSVNRRK
HHHHHHHHHHHHHCC		24.5221963094
528SumoylationVSLKMQLKQSVNRRK
HHHHHHHHHHHHHCC		24.5228112733
530PhosphorylationLKMQLKQSVNRRKMP
HHHHHHHHHHHCCCC		21.55-
548UbiquitinationRDHCKVSKSAHSLQP
HCCHHHCCCHHHCCC		55.4322505724
556PhosphorylationSAHSLQPSISQKSVF
CHHHCCCCCCHHHHH		23.1629449344
558PhosphorylationHSLQPSISQKSVFQM
HHCCCCCCHHHHHHH		35.5725159151
560UbiquitinationLQPSISQKSVFQMFQ
CCCCCCHHHHHHHHH		41.6221963094
560AcetylationLQPSISQKSVFQMFQ
CCCCCCHHHHHHHHH		41.6225953088
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
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:32416261
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN168_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 RN168_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A2C_HUMANHIST2H2ACphysical
19203578
H2AX_HUMANH2AFXphysical
19500350
UBE2N_HUMANUBE2Nphysical
20725033
H2A2C_HUMANHIST2H2ACphysical
21041483
H2A2A_HUMANHIST2H2AA3physical
21041483
H2B2E_HUMANHIST2H2BEphysical
21041483
HERC2_HUMANHERC2physical
20023648
KDM4A_HUMANKDM4Aphysical
22373579
H2A2C_HUMANHIST2H2ACphysical
22492721
UBC_HUMANUBCphysical
22742833
ECM29_HUMANKIAA0368physical
20682791
UBE2N_HUMANUBE2Nphysical
19203578
UB2D3_HUMANUBE2D3physical
22373579
UB2E1_HUMANUBE2E1physical
22492721
UB2D3_HUMANUBE2D3physical
19500350
POC1A_HUMANPOC1Aphysical
22939629
SMCA5_HUMANSMARCA5physical
23264744
UBE2N_HUMANUBE2Nphysical
23255131
H2A2C_HUMANHIST2H2ACphysical
22980979
UBR5_HUMANUBR5physical
22884692
TRIPC_HUMANTRIP12physical
22884692
KDM1A_HUMANKDM1Aphysical
24217620
JHD2C_HUMANJMJD1Cphysical
24240613
BCL10_HUMANBCL10physical
24732096
RN168_HUMANRNF168physical
19203578
UBC_HUMANUBCphysical
22266820
KDM1A_HUMANKDM1Aphysical
25999347
PSD11_HUMANPSMD11physical
26496610
TBP_HUMANTBPphysical
26496610
SRCAP_HUMANSRCAPphysical
26496610
CC174_HUMANCCDC174physical
26496610
NUB1_HUMANNUB1physical
26496610
RPR1B_HUMANRPRD1Bphysical
26496610
FA45A_HUMANFAM45Aphysical
26496610
SUMO2_HUMANSUMO2physical
26675234
SUMO3_HUMANSUMO3physical
26675234
UBC_HUMANUBCphysical
26503038
H12_HUMANHIST1H1Cphysical
26503038
UB2D1_HUMANUBE2D1physical
26508657
H2AZ_HUMANH2AFZphysical
26508657
FOXM1_HUMANFOXM1physical
27526106
PALB2_HUMANPALB2physical
28240985
BRCA2_HUMANBRCA2physical
28240985
UBC_HUMANUBCphysical
28240985
TOP2A_HUMANTOP2Aphysical
27558965
KI67_HUMANMKI67physical
27558965
SUMO1_HUMANSUMO1physical
27558965
UBB_HUMANUBBphysical
27558965
ZO1_HUMANTJP1physical
27558965
PCM1_HUMANPCM1physical
27558965
RRP5_HUMANPDCD11physical
27558965
NUCL_HUMANNCLphysical
27558965
HNRPM_HUMANHNRNPMphysical
27558965
DDX21_HUMANDDX21physical
27558965
RAI14_HUMANRAI14physical
27558965
LIMA1_HUMANLIMA1physical
27558965
DHX9_HUMANDHX9physical
27558965
DHX15_HUMANDHX15physical
27558965
DREB_HUMANDBN1physical
27558965
PABP4_HUMANPABPC4physical
27558965
UBP10_HUMANUSP10physical
27558965
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611943Riddle syndrome (RIDDLES)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN168_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-411; SER-414 ANDSER-415, AND MASS 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-411; SER-414; SER-415AND THR-421, AND MASS SPECTROMETRY.

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