RN168_MOUSE - dbPTM
RN168_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN168_MOUSE
UniProt AC Q80XJ2
Protein Name E3 ubiquitin-protein ligase RNF168 {ECO:0000255|HAMAP-Rule:MF_03066}
Gene Name Rnf168 {ECO:0000255|HAMAP-Rule:MF_03066}
Organism Mus musculus (Mouse).
Sequence Length 565
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 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 MAAPKTSIPSLAECQCGICMEILLEPVTLPCNHTLCNPCFQSTVEKANLCCPFCRRRVSSWTRYHTRRNSLVNTDLWEIIQKHYAKECKLRISGQESKEIIDECQPVRRLSEPGELRREYEEEISRVEAERQASKEEENKASEEYIQRLLAEEEEEEKRQREKRRSEMEEQLRGDEELARSLSTSINSNYERNTLASPLSSRKSDPVTNKSQKKNTSKQKTFGDIQKYLSPKLKPGTALACKAELEEDICKSKETDRSDTKSPVLQDTEIEKNIPTLSPQTCLETQEQGSESSAGIPGPQLCVGDTKESLEGKVETVSTSPDDLCIVNDDGPRATVFYSNEAAVNSSSKIENEEYSVTGVPQLTGGNRVPTESRVYHLLVEEEISDRENQESVFEEVMDPCFSAKRRKIFIESSSDQEETEVNFTQKLIDLEHMLFERHKQEEQDRLLALQLQKEVDKEQMVPNRQKGSPDQYQLRTPSPPDRLLNRQRKNSKDRNSLQQTNADHSKSPRNTKGDYWEPFKNTWKDSVNGTKMPTSTQDNCNVSKSAYTVQHRKSQRSIVQMFQR
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
70PhosphorylationRYHTRRNSLVNTDLW
HHHHHCCCCCCHHHH
31.7026643407
111PhosphorylationCQPVRRLSEPGELRR
CCCCCCCCCCCHHHH
39.6826824392
120PhosphorylationPGELRREYEEEISRV
CCHHHHHHHHHHHHH
27.1628285833
134PhosphorylationVEAERQASKEEENKA
HHHHHHHCHHHHHHH
32.06-
197PhosphorylationYERNTLASPLSSRKS
CCCCCCCCCCCCCCC
29.5026643407
200PhosphorylationNTLASPLSSRKSDPV
CCCCCCCCCCCCCCC
31.3324759943
201PhosphorylationTLASPLSSRKSDPVT
CCCCCCCCCCCCCCC
51.9526643407
251UbiquitinationELEEDICKSKETDRS
HHHHHHHHCCCCCCC
65.97-
252PhosphorylationLEEDICKSKETDRSD
HHHHHHHCCCCCCCC
31.1729899451
258PhosphorylationKSKETDRSDTKSPVL
HCCCCCCCCCCCCCC
53.0625619855
260PhosphorylationKETDRSDTKSPVLQD
CCCCCCCCCCCCCCC
34.3725619855
262PhosphorylationTDRSDTKSPVLQDTE
CCCCCCCCCCCCCCH
23.4925521595
268PhosphorylationKSPVLQDTEIEKNIP
CCCCCCCCHHHHHCC
26.3822817900
276PhosphorylationEIEKNIPTLSPQTCL
HHHHHCCCCCHHHHH
35.7525619855
278PhosphorylationEKNIPTLSPQTCLET
HHHCCCCCHHHHHHC
19.8925619855
281PhosphorylationIPTLSPQTCLETQEQ
CCCCCHHHHHHCHHC
23.5725619855
285PhosphorylationSPQTCLETQEQGSES
CHHHHHHCHHCCCCC
25.1825619855
290PhosphorylationLETQEQGSESSAGIP
HHCHHCCCCCCCCCC
33.7225619855
292PhosphorylationTQEQGSESSAGIPGP
CHHCCCCCCCCCCCC
27.4725619855
313UbiquitinationTKESLEGKVETVSTS
CHHHHCCCEEEEECC
27.76-
318PhosphorylationEGKVETVSTSPDDLC
CCCEEEEECCCCCEE
30.5028066266
319PhosphorylationGKVETVSTSPDDLCI
CCEEEEECCCCCEEE
39.6928066266
320PhosphorylationKVETVSTSPDDLCIV
CEEEEECCCCCEEEE
20.8728066266
346PhosphorylationSNEAAVNSSSKIENE
CCCCCCCCCCCCCCC
29.4125619855
347PhosphorylationNEAAVNSSSKIENEE
CCCCCCCCCCCCCCE
30.3725619855
348PhosphorylationEAAVNSSSKIENEEY
CCCCCCCCCCCCCEE
37.1625619855
413PhosphorylationRRKIFIESSSDQEET
CCEEEEECCCCCCCH
30.2626643407
414PhosphorylationRKIFIESSSDQEETE
CEEEEECCCCCCCHH
25.7426643407
415PhosphorylationKIFIESSSDQEETEV
EEEEECCCCCCCHHH
53.2226643407
420PhosphorylationSSSDQEETEVNFTQK
CCCCCCCHHHCHHHH
44.4726643407
469PhosphorylationVPNRQKGSPDQYQLR
CCCCCCCCCCCCCCC
32.1328066266
477PhosphorylationPDQYQLRTPSPPDRL
CCCCCCCCCCCHHHH
36.3925338131
479PhosphorylationQYQLRTPSPPDRLLN
CCCCCCCCCHHHHHH
48.7527149854
501PhosphorylationDRNSLQQTNADHSKS
CHHHHHHHCCCCCCC
21.2928066266
506PhosphorylationQQTNADHSKSPRNTK
HHHCCCCCCCCCCCC
35.0628066266
508PhosphorylationTNADHSKSPRNTKGD
HCCCCCCCCCCCCCC
31.9125266776
510MethylationADHSKSPRNTKGDYW
CCCCCCCCCCCCCCC
71.2216186413
513UbiquitinationSKSPRNTKGDYWEPF
CCCCCCCCCCCCHHC
54.02-
527PhosphorylationFKNTWKDSVNGTKMP
CCCCCCCCCCCCCCC
17.4728059163

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 RN168_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN168_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TP53B_MOUSETrp53bp1physical
24324146
MDC1_MOUSEMdc1physical
24324146

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN168_MOUSE

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Related Literatures of Post-Translational Modification

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