XRCC5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XRCC5_MOUSE
• UniProt AC: P27641
• Protein Name: X-ray repair cross-complementing protein 5
• Gene Name: Xrcc5
• Organism: Mus musculus (Mouse).
• Sequence Length: 732
• Subcellular Localization: Nucleus . Nucleus, nucleolus . Chromosome .
• Protein Description: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway..
• Protein Sequence: MAWSGNKAAVVLCVDVGVAMGNSFPGEESPIEQAKKVMTMFVQRQVFSESKDEIALVLYGTDGTDNALAGKDQYQNITVCRHLMLPDFDLLEDIGNKIQPSSQQADFLDALIVCMDLIQRETIGKKFGKKHIEVFTDLSSPFSQDQLDVIICNLKKSGISLQFFLPFPIDKNGEPGERGDLDSGLDHLKPSFPQKGLTEQQKEGIRMVTRVMLSLEGEDGLDEIYSFSESLRQLCVFKKIERRSMPWPCQLTIGPNLSIKIVAYKSIVQEKFKKSWVVVDARTLKKEDIQKETVYCLNDDDETEVSKEDTIQGYRYGSDIIPFSKVDEEQMKYKSEGKCFSVLGFCKSSQVHRRFFMGHQVLKVFAAKDDEAAAVALSSLVHALDELNMVAIVRYAYDKRSNPQVGVAFPYIKDAYECLVYVQLPFMEDLRQYMFSSLKNNKKCTPTEAQLSAIDDLIDSMSLVKKNEEEDIVEDLFPTSKIPNPEFQRLYQCLLHRALHLQERLPPIQQHILNMLDPPTEMKAKCESPLSKVKTLFPLTEVIKKKNQVTAQDVFQDNHEEGPAAKKYKTEKEEDHISISSLAEGNITKVGSVNPVENFRFLVRQKIASFEEASLQLISHIEQFLDTNETLYFMKSMDCIKAFREEAIQFSEEQRFNSFLEALREKVEIKQLNHFWEIVVQDGVTLITKDEGPGSSITAEEATKFLAPKDKAKEDTTGPEEAGDVDDLLDMI

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
244	Phosphorylation	FKKIERRSMPWPCQL HHHCCCCCCCCCCEE	35.10	26643407
258	Phosphorylation	LTIGPNLSIKIVAYK EEECCCCEEEEEEEH	28.60	-
265	Acetylation	SIKIVAYKSIVQEKF EEEEEEEHHHHHHHH	24.78	23236377
265	Malonylation	SIKIVAYKSIVQEKF EEEEEEEHHHHHHHH	24.78	26320211
275	Phosphorylation	VQEKFKKSWVVVDAR HHHHHHCCEEEEECC	26.20	29899451
283	Phosphorylation	WVVVDARTLKKEDIQ EEEEECCCCCHHHCC	44.65	29899451
306	Ubiquitination	DDDETEVSKEDTIQG CCCCCEECHHHCCCC	24.89	27667366
316	Phosphorylation	DTIQGYRYGSDIIPF HCCCCCCCCCCEECH	16.70	26643407
318	Phosphorylation	IQGYRYGSDIIPFSK CCCCCCCCCEECHHH	19.39	26643407
324	Phosphorylation	GSDIIPFSKVDEEQM CCCEECHHHCCHHHH	26.81	26643407
325	Ubiquitination	SDIIPFSKVDEEQMK CCEECHHHCCHHHHC	54.83	22790023
332	Acetylation	KVDEEQMKYKSEGKC HCCHHHHCCCCCCCE	49.58	7713933
333	Phosphorylation	VDEEQMKYKSEGKCF CCHHHHCCCCCCCEE	17.88	26643407
528	Phosphorylation	EMKAKCESPLSKVKT HHHHHCCCCHHHHHH	40.38	28833060
531	Phosphorylation	AKCESPLSKVKTLFP HHCCCCHHHHHHHHH	38.49	28066266
535	Phosphorylation	SPLSKVKTLFPLTEV CCHHHHHHHHHHHHH	36.30	-
544	Ubiquitination	FPLTEVIKKKNQVTA HHHHHHHHHCCCCCH	63.97	22790023
578	Phosphorylation	EKEEDHISISSLAEG CCCCCCEEHHHHHCC	17.01	10026262
580	Phosphorylation	EEDHISISSLAEGNI CCCCEEHHHHHCCCC	16.71	-
581	Phosphorylation	EDHISISSLAEGNIT CCCEEHHHHHCCCCE	29.90	10026262
592	Phosphorylation	GNITKVGSVNPVENF CCCEEEECCCCCCCH	23.00	23140645
666	Acetylation	FLEALREKVEIKQLN HHHHHHHHHCHHHHC	38.44	-
716	Phosphorylation	KDKAKEDTTGPEEAG CCCCCCCCCCHHHCC	34.44	10026262
717	Phosphorylation	DKAKEDTTGPEEAGD CCCCCCCCCHHHCCC	64.16	25338131

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
578	S	Phosphorylation	Kinase	PRKDC	P97313	Uniprot
580	S	Phosphorylation	Kinase	PRKDC	P97313	Uniprot
581	S	Phosphorylation	Kinase	PRKDC	P97313	Uniprot
716	T	Phosphorylation	Kinase	PRKDC	P97313	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of XRCC5_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of XRCC5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERF1_MOUSE	Terf1	genetic	22556254
TERF2_MOUSE	Terf2	genetic	22556254

Drug and Disease Associations

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