dbPTM

XRCC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XRCC1_MOUSE
UniProt AC	Q60596
Protein Name	DNA repair protein XRCC1
Gene Name	Xrcc1
Organism	Mus musculus (Mouse).
Sequence Length	631
Subcellular Localization	Nucleus . Nucleus, nucleolus . Moves from the nucleoli to the global nuclear chromatin upon DNA damage.
Protein Description	Involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (By similarity). Probably during DNA repair, negatively regulates ADP-ribose levels by modulating ADP-ribosyltransferase PARP1 activity. [PubMed: 28002403]
Protein Sequence	MPEISLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSAGGATAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRIFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPYGLSFVKFHSPPDKDEAEATSQKVTVTKLGQFRVKEEDDSANSLKPGALFFSRINKTSSASTSDPAGPSYAAATLQASSAASSASPVPKVVGSSSKPQEPPKGKRKLDLSLEDRKPPSKPSAGPSTLKRPKLSVPSRTPAAAPASTPAQRAVPGKPRGEGTEPRGARTGPQELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTPDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHHMRRRLPSRRYLMAGLGSSSEDEGDSHSESGEDEAPKLPQKRPQPKAKTQAAGPSSPPRPPTPKETKAPSPGPQDNSDTEGEESEGRDNGAEDSGDTEDELRRVAKQREQRQPPAPEENGEDPYAGSTDENTDSETPSEADLPIPELPDFFEGKHFFLYGEFPGDERRRLIRYVTAFNGELEDYMNERVQFVITAQEWDPNFEEALMENPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MPEISLRHVVSC ---CCCCCEEEEEEC	20.07	29895711
11	Phosphorylation	ISLRHVVSCSSQDST CCEEEEEECCCCCCH	13.75	29895711
142	Phosphorylation	SQPYSKDSPYGLSFV CCCCCCCCCCCCEEE	24.61	-
171	Acetylation	SQKVTVTKLGQFRVK CCEEEEEEEEEEEEE	46.41	23806337
200	Phosphorylation	FFSRINKTSSASTSD EEEECCCCCCCCCCC	24.35	25619855
201	Phosphorylation	FSRINKTSSASTSDP EEECCCCCCCCCCCC	26.05	25619855
202	Phosphorylation	SRINKTSSASTSDPA EECCCCCCCCCCCCC	31.32	25619855
204	Phosphorylation	INKTSSASTSDPAGP CCCCCCCCCCCCCCC	30.32	25619855
205	Phosphorylation	NKTSSASTSDPAGPS CCCCCCCCCCCCCCC	36.54	25619855
206	Phosphorylation	KTSSASTSDPAGPSY CCCCCCCCCCCCCCH	38.82	25619855
212	Phosphorylation	TSDPAGPSYAAATLQ CCCCCCCCHHHHHHH	26.87	25619855
213	Phosphorylation	SDPAGPSYAAATLQA CCCCCCCHHHHHHHH	11.91	25619855
217	Phosphorylation	GPSYAAATLQASSAA CCCHHHHHHHHHHHH	18.06	25619855
221	Phosphorylation	AAATLQASSAASSAS HHHHHHHHHHHHCCC	13.93	25619855
222	Phosphorylation	AATLQASSAASSASP HHHHHHHHHHHCCCC	30.76	25619855
225	Phosphorylation	LQASSAASSASPVPK HHHHHHHHCCCCCCC	26.59	25619855
226	Phosphorylation	QASSAASSASPVPKV HHHHHHHCCCCCCCC	28.21	25619855
228	Phosphorylation	SSAASSASPVPKVVG HHHHHCCCCCCCCCC	28.51	22942356
253	Phosphorylation	GKRKLDLSLEDRKPP CCCCCCCCCCCCCCC	29.40	28066266
261	Phosphorylation	LEDRKPPSKPSAGPS CCCCCCCCCCCCCCC	66.77	-
264	Phosphorylation	RKPPSKPSAGPSTLK CCCCCCCCCCCCCCC	49.98	22817900
276	Phosphorylation	TLKRPKLSVPSRTPA CCCCCCCCCCCCCCC	37.80	24719451
281	Phosphorylation	KLSVPSRTPAAAPAS CCCCCCCCCCCCCCC	22.93	-
371	Phosphorylation	FANTPKYSQVLGLGG ECCCCCHHHHCCCCC	21.68	-
408	Phosphorylation	YLMAGLGSSSEDEGD HEEECCCCCCCCCCC	35.42	28285833
409	Phosphorylation	LMAGLGSSSEDEGDS EEECCCCCCCCCCCC	35.63	28285833
410	Phosphorylation	MAGLGSSSEDEGDSH EECCCCCCCCCCCCC	51.25	-
418	Phosphorylation	EDEGDSHSESGEDEA CCCCCCCCCCCCCCC	37.09	28285833
439	Phosphorylation	RPQPKAKTQAAGPSS CCCCCCCCCCCCCCC	28.44	25619855
445	Phosphorylation	KTQAAGPSSPPRPPT CCCCCCCCCCCCCCC	55.34	25521595
446	Phosphorylation	TQAAGPSSPPRPPTP CCCCCCCCCCCCCCC	41.90	27087446
452	Phosphorylation	SSPPRPPTPKETKAP CCCCCCCCCCCCCCC	50.07	27087446
456	Phosphorylation	RPPTPKETKAPSPGP CCCCCCCCCCCCCCC	38.34	24759943
460	Phosphorylation	PKETKAPSPGPQDNS CCCCCCCCCCCCCCC	47.55	25195567
467	Phosphorylation	SPGPQDNSDTEGEES CCCCCCCCCCCCCCC	54.95	21149613
469	Phosphorylation	GPQDNSDTEGEESEG CCCCCCCCCCCCCCC	45.79	21149613
474	Phosphorylation	SDTEGEESEGRDNGA CCCCCCCCCCCCCCC	40.84	25338131
484	Phosphorylation	RDNGAEDSGDTEDEL CCCCCCCCCCCHHHH	30.03	25521595
487	Phosphorylation	GAEDSGDTEDELRRV CCCCCCCCHHHHHHH	49.19	25521595
514	Phosphorylation	EENGEDPYAGSTDEN CCCCCCCCCCCCCCC	35.60	24224561
517	Phosphorylation	GEDPYAGSTDENTDS CCCCCCCCCCCCCCC	25.23	24224561
518	Phosphorylation	EDPYAGSTDENTDSE CCCCCCCCCCCCCCC	46.55	24224561
522	Phosphorylation	AGSTDENTDSETPSE CCCCCCCCCCCCCCC	38.56	-
524	Phosphorylation	STDENTDSETPSEAD CCCCCCCCCCCCCCC	41.13	-
526	Phosphorylation	DENTDSETPSEADLP CCCCCCCCCCCCCCC	35.75	-

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 XRCC1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
371	S	Phosphorylation		-
Phosphorylation of Ser-371 causes dimer dissociation.

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 XRCC1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
REV1_HUMAN	REV1	physical	24409475

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of XRCC1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, ANDMASS SPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-487, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, ANDMASS SPECTROMETRY.	14729942 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, AND MASSSPECTROMETRY.	17242355 [Abstract]

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