XRCC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XRCC2_HUMAN
• UniProt AC: O43543
• Protein Name: DNA repair protein XRCC2
• Gene Name: XRCC2
• Organism: Homo sapiens (Human).
• Sequence Length: 280
• Subcellular Localization: Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
• Protein Description: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA..
• Protein Sequence: MCSAFHRAESGTELLARLEGRSSLKEIEPNLFADEDSPVHGDILEFHGPEGTGKTEMLYHLTARCILPKSEGGLEVEVLFIDTDYHFDMLRLVTILEHRLSQSSEEIIKYCLGRFFLVYCSSSTHLLLTLYSLESMFCSHPSLCLLILDSLSAFYWIDRVNGGESVNLQESTLRKCSQCLEKLVNDYRLVLFATTQTIMQKASSSSEEPSHASRRLCDVDIDYRPYLCKAWQQLVKHRMFFSKQDDSQSSNQFSLVSRCLKSNSLKKHFFIIGESGVEFC

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
10	Phosphorylation	SAFHRAESGTELLAR CCCCCCCCHHHHHHH	50.45	23401153
12	Phosphorylation	FHRAESGTELLARLE CCCCCCHHHHHHHHH	32.51	29523821
22	Phosphorylation	LARLEGRSSLKEIEP HHHHHCCCCCCCCCC	51.37	23898821
25	Ubiquitination	LEGRSSLKEIEPNLF HHCCCCCCCCCCCCC	59.60	-
59	Phosphorylation	TGKTEMLYHLTARCI CCHHHHHHEEEEEEE	8.09	-
236	Ubiquitination	KAWQQLVKHRMFFSK HHHHHHHHHHHHCCC	33.80	-
243	Ubiquitination	KHRMFFSKQDDSQSS HHHHHCCCCCCCCCC	53.22	2190698
247	Phosphorylation	FFSKQDDSQSSNQFS HCCCCCCCCCCCHHH	40.01	17525332
249	Phosphorylation	SKQDDSQSSNQFSLV CCCCCCCCCCHHHHH	34.90	17525332
261	Ubiquitination	SLVSRCLKSNSLKKH HHHHHHHHCCCCCCE	51.74	-
262	Phosphorylation	LVSRCLKSNSLKKHF HHHHHHHCCCCCCEE	20.78	29083192
264	Phosphorylation	SRCLKSNSLKKHFFI HHHHHCCCCCCEEEE	48.97	29083192

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
247	S	Phosphorylation	Kinase	ATR	Q13535	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of XRCC2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of XRCC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RA51D_HUMAN	RAD51D	physical	10749867
BLM_HUMAN	BLM	physical	12975363
RA51C_HUMAN	RAD51C	physical	26186194
RA51B_HUMAN	RAD51B	physical	26186194
RA51D_HUMAN	RAD51D	physical	26186194
RA51D_HUMAN	RAD51D	physical	27161866
RA51D_HUMAN	RAD51D	physical	28514442
RA51B_HUMAN	RAD51B	physical	28514442
RA51C_HUMAN	RAD51C	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-249, ANDMASS SPECTROMETRY.
PubMed: 17525332