XRCC6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XRCC6_MOUSE
• UniProt AC: P23475
• Protein Name: X-ray repair cross-complementing protein 6
• Gene Name: Xrcc6
• Organism: Mus musculus (Mouse).
• Sequence Length: 608
• Subcellular Localization: Nucleus. 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. Required for osteocalcin gene expression. 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. 5'-dRP lyase activity 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 (By similarity)..
• Protein Sequence: MSEWESYYKTEGEEEEEEEESPDTGGEYKYSGRDSLIFLVDASRAMFESQGEDELTPFDMSIQCIQSVYTSKIISSDRDLLAVVFYGTEKDKNSVNFKNIYVLQDLDNPGAKRVLELDQFKGQQGKKHFRDTVGHGSDYSLSEVLWVCANLFSDVQLKMSHKRIMLFTNEDDPHGRDSAKASRARTKASDLRDTGIFLDLMHLKKPGGFDVSVFYRDIITTAEDEDLGVHFEESSKLEDLLRKVRAKETKKRVLSRLKFKLGEDVVLMVGIYNLVQKANKPFPVRLYRETNEPVKTKTRTFNVNTGSLLLPSDTKRSLTYGTRQIVLEKEETEELKRFDEPGLILMGFKPTVMLKKQHYLRPSLFVYPEESLVSGSSTLFSALLTKCVEKKVIAVCRYTPRKNVSPYFVALVPQEEELDDQNIQVTPGGFQLVFLPYADDKRKVPFTEKVTANQEQIDKMKAIVQKLRFTYRSDSFENPVLQQHFRNLEALALDMMESEQVVDLTLPKVEAIKKRLGSLADEFKELVYPPGYNPEGKVAKRKQDDEGSTSKKPKVELSEEELKAHFRKGTLGKLTVPTLKDICKAHGLKSGPKKQELLDALIRHLEKN

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
2	Phosphorylation	------MSEWESYYK ------CCCHHCCCC	51.95	29514104
2	Acetylation	------MSEWESYYK ------CCCHHCCCC	51.95	-
6	Phosphorylation	--MSEWESYYKTEGE --CCCHHCCCCCCCC	34.53	19664609
29	Acetylation	PDTGGEYKYSGRDSL CCCCCCCEECCCCEE	28.74	23954790
49	Phosphorylation	ASRAMFESQGEDELT HHHHHHHHCCCCCCC	32.02	19664609
290	Phosphorylation	PVRLYRETNEPVKTK CEEEEECCCCCCCCE	35.56	24719451
307	Phosphorylation	TFNVNTGSLLLPSDT EEECCCCCEECCCCC	17.51	24719451
329	Acetylation	TRQIVLEKEETEELK CEEEEEEHHHHHHHH	57.60	-
336	Acetylation	KEETEELKRFDEPGL HHHHHHHHCCCCCCE	55.06	-
451	Phosphorylation	VPFTEKVTANQEQID CCCCCCCCCCHHHHH	30.84	26060331
459	Acetylation	ANQEQIDKMKAIVQK CCHHHHHHHHHHHHH	43.88	-
470	Phosphorylation	IVQKLRFTYRSDSFE HHHHHHCEECCCCCC	16.16	26643407
471	Phosphorylation	VQKLRFTYRSDSFEN HHHHHCEECCCCCCC	12.86	26643407
473	Phosphorylation	KLRFTYRSDSFENPV HHHCEECCCCCCCHH	27.48	26643407
475	Phosphorylation	RFTYRSDSFENPVLQ HCEECCCCCCCHHHH	35.39	28507225
518	Phosphorylation	AIKKRLGSLADEFKE HHHHHHCCHHHHHHH	25.61	27087446
548	Phosphorylation	RKQDDEGSTSKKPKV CCCCCCCCCCCCCCC	27.71	-
558	Phosphorylation	KKPKVELSEEELKAH CCCCCCCCHHHHHHH	29.47	29899451

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
6	S	Phosphorylation	Kinase	PRKDC	P97313	Uniprot
49	S	Phosphorylation	Kinase	PRKDC	P97313	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
49	S	Phosphorylation	Phosphorylation of Ser-49 does not affect DNA repair.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of XRCC6_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of XRCC6_MOUSE !!

Drug and Disease Associations

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