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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
70 | Phosphorylation | RYHTRRNSLVNTDLW HHHHHCCCCCCHHHH | 31.70 | 26643407 | |
111 | Phosphorylation | CQPVRRLSEPGELRR CCCCCCCCCCCHHHH | 39.68 | 26824392 | |
120 | Phosphorylation | PGELRREYEEEISRV CCHHHHHHHHHHHHH | 27.16 | 28285833 | |
134 | Phosphorylation | VEAERQASKEEENKA HHHHHHHCHHHHHHH | 32.06 | - | |
197 | Phosphorylation | YERNTLASPLSSRKS CCCCCCCCCCCCCCC | 29.50 | 26643407 | |
200 | Phosphorylation | NTLASPLSSRKSDPV CCCCCCCCCCCCCCC | 31.33 | 24759943 | |
201 | Phosphorylation | TLASPLSSRKSDPVT CCCCCCCCCCCCCCC | 51.95 | 26643407 | |
251 | Ubiquitination | ELEEDICKSKETDRS HHHHHHHHCCCCCCC | 65.97 | - | |
252 | Phosphorylation | LEEDICKSKETDRSD HHHHHHHCCCCCCCC | 31.17 | 29899451 | |
258 | Phosphorylation | KSKETDRSDTKSPVL HCCCCCCCCCCCCCC | 53.06 | 25619855 | |
260 | Phosphorylation | KETDRSDTKSPVLQD CCCCCCCCCCCCCCC | 34.37 | 25619855 | |
262 | Phosphorylation | TDRSDTKSPVLQDTE CCCCCCCCCCCCCCH | 23.49 | 25521595 | |
268 | Phosphorylation | KSPVLQDTEIEKNIP CCCCCCCCHHHHHCC | 26.38 | 22817900 | |
276 | Phosphorylation | EIEKNIPTLSPQTCL HHHHHCCCCCHHHHH | 35.75 | 25619855 | |
278 | Phosphorylation | EKNIPTLSPQTCLET HHHCCCCCHHHHHHC | 19.89 | 25619855 | |
281 | Phosphorylation | IPTLSPQTCLETQEQ CCCCCHHHHHHCHHC | 23.57 | 25619855 | |
285 | Phosphorylation | SPQTCLETQEQGSES CHHHHHHCHHCCCCC | 25.18 | 25619855 | |
290 | Phosphorylation | LETQEQGSESSAGIP HHCHHCCCCCCCCCC | 33.72 | 25619855 | |
292 | Phosphorylation | TQEQGSESSAGIPGP CHHCCCCCCCCCCCC | 27.47 | 25619855 | |
313 | Ubiquitination | TKESLEGKVETVSTS CHHHHCCCEEEEECC | 27.76 | - | |
318 | Phosphorylation | EGKVETVSTSPDDLC CCCEEEEECCCCCEE | 30.50 | 28066266 | |
319 | Phosphorylation | GKVETVSTSPDDLCI CCEEEEECCCCCEEE | 39.69 | 28066266 | |
320 | Phosphorylation | KVETVSTSPDDLCIV CEEEEECCCCCEEEE | 20.87 | 28066266 | |
346 | Phosphorylation | SNEAAVNSSSKIENE CCCCCCCCCCCCCCC | 29.41 | 25619855 | |
347 | Phosphorylation | NEAAVNSSSKIENEE CCCCCCCCCCCCCCE | 30.37 | 25619855 | |
348 | Phosphorylation | EAAVNSSSKIENEEY CCCCCCCCCCCCCEE | 37.16 | 25619855 | |
413 | Phosphorylation | RRKIFIESSSDQEET CCEEEEECCCCCCCH | 30.26 | 26643407 | |
414 | Phosphorylation | RKIFIESSSDQEETE CEEEEECCCCCCCHH | 25.74 | 26643407 | |
415 | Phosphorylation | KIFIESSSDQEETEV EEEEECCCCCCCHHH | 53.22 | 26643407 | |
420 | Phosphorylation | SSSDQEETEVNFTQK CCCCCCCHHHCHHHH | 44.47 | 26643407 | |
469 | Phosphorylation | VPNRQKGSPDQYQLR CCCCCCCCCCCCCCC | 32.13 | 28066266 | |
477 | Phosphorylation | PDQYQLRTPSPPDRL CCCCCCCCCCCHHHH | 36.39 | 25338131 | |
479 | Phosphorylation | QYQLRTPSPPDRLLN CCCCCCCCCHHHHHH | 48.75 | 27149854 | |
501 | Phosphorylation | DRNSLQQTNADHSKS CHHHHHHHCCCCCCC | 21.29 | 28066266 | |
506 | Phosphorylation | QQTNADHSKSPRNTK HHHCCCCCCCCCCCC | 35.06 | 28066266 | |
508 | Phosphorylation | TNADHSKSPRNTKGD HCCCCCCCCCCCCCC | 31.91 | 25266776 | |
510 | Methylation | ADHSKSPRNTKGDYW CCCCCCCCCCCCCCC | 71.22 | 16186413 | |
513 | Ubiquitination | SKSPRNTKGDYWEPF CCCCCCCCCCCCHHC | 54.02 | - | |
527 | Phosphorylation | FKNTWKDSVNGTKMP CCCCCCCCCCCCCCC | 17.47 | 28059163 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RN168_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TP53B_MOUSE | Trp53bp1 | physical | 24324146 | |
MDC1_MOUSE | Mdc1 | physical | 24324146 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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