dbPTM

XRCC4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XRCC4_HUMAN
UniProt AC	Q13426
Protein Name	DNA repair protein XRCC4
Gene Name	XRCC4
Organism	Homo sapiens (Human).
Sequence Length	336
Subcellular Localization	Nucleus .
Protein Description	Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends..
Protein Sequence	MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MERKISRIHLVSE --CCCCCCEEEECCC	28.37	-
17	Phosphorylation	LVSEPSITHFLQVSW ECCCCCCCEEEEEEH	15.77	-
65	Ubiquitination	DMAMEKGKYVGELRK HHHHHHCCHHHHHHH	48.07	-
65	Acetylation	DMAMEKGKYVGELRK HHHHHHCCHHHHHHH	48.07	25953088
76	Phosphorylation	ELRKALLSGAGPADV HHHHHHHHCCCCCCE	27.70	21406692
84	Phosphorylation	GAGPADVYTFNFSKE CCCCCCEEEEECCCC	13.22	21406692
85	Phosphorylation	AGPADVYTFNFSKES CCCCCEEEEECCCCC	16.38	21406692
89	Phosphorylation	DVYTFNFSKESCYFF CEEEEECCCCCEEEE	36.30	21406692
102	Ubiquitination	FFFEKNLKDVSFRLG EEEECCCCCCEEEEC	66.53	21906983
102 (in isoform 3)	Ubiquitination	-	66.53	21890473
102 (in isoform 2)	Ubiquitination	-	66.53	21890473
102 (in isoform 1)	Ubiquitination	-	66.53	21890473
146	Ubiquitination	AKNEHLQKENERLLR HHHHHHHHHHHHHHH	69.71	21906983
146 (in isoform 3)	Ubiquitination	-	69.71	21890473
146 (in isoform 2)	Ubiquitination	-	69.71	21890473
146 (in isoform 1)	Ubiquitination	-	69.71	21890473
164	Ubiquitination	DVQGRFEKCVSAKEA HHCHHHHHCCCHHHH	36.91	-
169	Ubiquitination	FEKCVSAKEALETDL HHHCCCHHHHHHCCH	35.69	-
178	Ubiquitination	ALETDLYKRFILVLN HHHCCHHHHHHHHHC	48.40	21906983
178	2-Hydroxyisobutyrylation	ALETDLYKRFILVLN HHHCCHHHHHHHHHC	48.40	-
178 (in isoform 1)	Ubiquitination	-	48.40	21890473
178 (in isoform 2)	Ubiquitination	-	48.40	21890473
178 (in isoform 3)	Ubiquitination	-	48.40	21890473
188	Ubiquitination	ILVLNEKKTKIRSLH HHHHCCCHHHHHHHH	49.20	-
193	Phosphorylation	EKKTKIRSLHNKLLN CCHHHHHHHHHHHHH	37.14	14599745
197	Acetylation	KIRSLHNKLLNAAQE HHHHHHHHHHHHHHH	43.53	25953088
197	Malonylation	KIRSLHNKLLNAAQE HHHHHHHHHHHHHHH	43.53	26320211
197 (in isoform 1)	Ubiquitination	-	43.53	21890473
197 (in isoform 2)	Ubiquitination	-	43.53	21890473
197 (in isoform 3)	Ubiquitination	-	43.53	21890473
197	Ubiquitination	KIRSLHNKLLNAAQE HHHHHHHHHHHHHHH	43.53	21890473
210	Sumoylation	QEREKDIKQEGETAI HHHHHHHHHHCCCEE	53.05	-
210	Sumoylation	QEREKDIKQEGETAI HHHHHHHHHHCCCEE	53.05	16478998
215	Phosphorylation	DIKQEGETAICSEMT HHHHHCCCEECCCCC	31.98	30576142
219	Phosphorylation	EGETAICSEMTADRD HCCCEECCCCCCCCC	25.04	30576142
222	Phosphorylation	TAICSEMTADRDPVY CEECCCCCCCCCCCC	22.73	30576142
229	Phosphorylation	TADRDPVYDESTDEE CCCCCCCCCCCCCHH	21.27	23663014
232	Phosphorylation	RDPVYDESTDEESEN CCCCCCCCCCHHHCC	37.96	21082442
233	Phosphorylation	DPVYDESTDEESENQ CCCCCCCCCHHHCCC	45.44	21082442
237	Phosphorylation	DESTDEESENQTDLS CCCCCHHHCCCCCCH	39.54	23663014
241	Phosphorylation	DEESENQTDLSGLAS CHHHCCCCCCHHHHH	50.95	23663014
244	Phosphorylation	SENQTDLSGLASAAV HCCCCCCHHHHHHHH	34.27	26074081
248	Phosphorylation	TDLSGLASAAVSKDD CCCHHHHHHHHCCCC	23.08	20363803
252	Phosphorylation	GLASAAVSKDDSIIS HHHHHHHCCCCCCHH	26.16	20363803
256 (in isoform 2)	Phosphorylation	-	31.77	-
256	Phosphorylation	AAVSKDDSIISSLDV HHHCCCCCCHHHCCC	31.77	29255136
259	Phosphorylation	SKDDSIISSLDVTDI CCCCCCHHHCCCCCC	24.15	23663014
260	Phosphorylation	KDDSIISSLDVTDIA CCCCCHHHCCCCCCC	20.41	25159151
264	Phosphorylation	IISSLDVTDIAPSRK CHHHCCCCCCCCCHH	22.73	23663014
282	Phosphorylation	RMQRNLGTEPKMAPQ HHHHHHCCCCCCCHH	52.89	23532336
286	Sulfoxidation	NLGTEPKMAPQENQL HHCCCCCCCHHHHHH	10.87	21406390
296	Ubiquitination	QENQLQEKENSRPDS HHHHHHHHHHCCCCC	49.59	-
299	Phosphorylation	QLQEKENSRPDSSLP HHHHHHHCCCCCCCC	46.40	29255136
301 (in isoform 2)	Phosphorylation	-	45.73	25159151
302 (in isoform 2)	Phosphorylation	-	50.15	25159151
303	Phosphorylation	KENSRPDSSLPETSK HHHCCCCCCCCCHHH	36.14	25849741
304	Phosphorylation	ENSRPDSSLPETSKK HHCCCCCCCCCHHHH	56.15	29255136
306 (in isoform 2)	Phosphorylation	-	44.78	26714015
308	Phosphorylation	PDSSLPETSKKEHIS CCCCCCCHHHHHHCC	43.86	23403867
309	Phosphorylation	DSSLPETSKKEHISA CCCCCCHHHHHHCCC	39.82	23403867
313 (in isoform 2)	Phosphorylation	-	28.34	-
315	Phosphorylation	TSKKEHISAENMSLE HHHHHHCCCCCCCHH	31.29	29255136
318 (in isoform 2)	Phosphorylation	-	25.67	-
320	Phosphorylation	HISAENMSLETLRNS HCCCCCCCHHHHHCC	34.34	29255136
321 (in isoform 2)	Phosphorylation	-	3.97	-
323	Phosphorylation	AENMSLETLRNSSPE CCCCCHHHHHCCCHH	35.99	29255136
325 (in isoform 2)	Phosphorylation	-	48.69	-
326 (in isoform 2)	Phosphorylation	-	50.37	-
327	Phosphorylation	SLETLRNSSPEDLFD CHHHHHCCCHHHHHH	40.61	25159151
328	Phosphorylation	LETLRNSSPEDLFDE HHHHHCCCHHHHHHC	35.54	25159151

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
233	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
260	S	Phosphorylation	Kinase	DNAPK	P78527	PSP
304	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
320	S	Phosphorylation	Kinase	DNAPK	P78527	PSP
327	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
328	S	Phosphorylation	Kinase	PRKDC	P78527	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
210	K	Sumoylation		16478998
Sumoylation at Lys-210 is required for nuclear localization and recombination efficiency.

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 XRCC4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IFFO1_HUMAN	IFFO1	physical	16189514
NHEJ1_HUMAN	NHEJ1	physical	17567543
XRCC4_HUMAN	XRCC4	physical	17567543
DNLI4_HUMAN	LIG4	physical	17567543
CHD3_HUMAN	CHD3	physical	16169070
VIME_HUMAN	VIM	physical	16169070
XRCC4_HUMAN	XRCC4	physical	16169070
PRKDC_HUMAN	PRKDC	physical	15520013
DNLI4_HUMAN	LIG4	physical	15520013
XRCC6_HUMAN	XRCC6	physical	15520013
XRCC5_HUMAN	XRCC5	physical	15520013
DNLI4_HUMAN	LIG4	physical	10757784
PRKDC_HUMAN	PRKDC	physical	15194694
BIN1_HUMAN	BIN1	physical	16275660
XRCC4_HUMAN	XRCC4	physical	25416956
ASTE1_HUMAN	ASTE1	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
AL7A1_HUMAN	ALDH7A1	physical	26186194
APTX_HUMAN	APTX	physical	26186194
DNLI4_HUMAN	LIG4	physical	26186194
IFFO2_HUMAN	IFFO2	physical	26186194
IFFO1_HUMAN	IFFO1	physical	26186194
NFKB1_HUMAN	NFKB1	physical	26186194
APBP2_HUMAN	APPBP2	physical	26186194
PNKP_HUMAN	PNKP	physical	26186194
LONF2_HUMAN	LONRF2	physical	26186194
XRCC4_HUMAN	XRCC4	physical	11080143
DNLI4_HUMAN	LIG4	physical	28514442
APTX_HUMAN	APTX	physical	28514442
IFFO2_HUMAN	IFFO2	physical	28514442
IFFO1_HUMAN	IFFO1	physical	28514442
PNKP_HUMAN	PNKP	physical	28514442
LONF2_HUMAN	LONRF2	physical	28514442
APBP2_HUMAN	APPBP2	physical	28514442
AL7A1_HUMAN	ALDH7A1	physical	28514442
NFKB1_HUMAN	NFKB1	physical	28514442
DNJC9_HUMAN	DNAJC9	physical	27173435
KIF3A_HUMAN	KIF3A	physical	27173435

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.

Regulatory Network of XRCC4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-328, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-328, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Identification of DNA-PKcs phosphorylation sites in XRCC4 and effectsof mutations at these sites on DNA end joining in a cell-freesystem."; Lee K.J., Jovanovic M., Udayakumar D., Bladen C.L., Dynan W.S.; DNA Repair 3:267-276(2004). Cited for: PHOSPHORYLATION AT SER-260 AND SER-320.	15177042 [Abstract]
Sumoylation
Reference	PubMed
"SUMO modification of human XRCC4 regulates its localization andfunction in DNA double-strand break repair."; Yurchenko V., Xue Z., Sadofsky M.J.; Mol. Cell. Biol. 26:1786-1794(2006). Cited for: SUMOYLATION AT LYS-210, SUBCELLULAR LOCATION, AND MUTAGENESIS OFLYS-140 AND LYS-210.	16478998 [Abstract]

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