XRCC3_HUMAN - dbPTM
XRCC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XRCC3_HUMAN
UniProt AC O43542
Protein Name DNA repair protein XRCC3
Gene Name XRCC3
Organism Homo sapiens (Human).
Sequence Length 346
Subcellular Localization Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair.
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 CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C..
Protein Sequence MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQRLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPRLRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGATLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSAPHLPPSSCSYTISAEGVRGTPGTQSH
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 Orthologous
Protein Cluster
1Acetylation-------MDLDLLDL
-------CCCCHHCC
11.8722814378
172-HydroxyisobutyrylationPRIIAAIKKAKLKSV
HHHHHHHHHHHCCCH
41.79-
18UbiquitinationRIIAAIKKAKLKSVK
HHHHHHHHHHCCCHH
44.64-
23PhosphorylationIKKAKLKSVKEVLHF
HHHHHCCCHHHHHHH
49.19-
25UbiquitinationKAKLKSVKEVLHFSG
HHHCCCHHHHHHHCC
49.55-
36UbiquitinationHFSGPDLKRLTNLSS
HHCCCCHHHHCCCCC
53.38-
39PhosphorylationGPDLKRLTNLSSPEV
CCCHHHHCCCCCHHH
37.8427732954
42PhosphorylationLKRLTNLSSPEVWHL
HHHHCCCCCHHHHHH
46.0124719451
43PhosphorylationKRLTNLSSPEVWHLL
HHHCCCCCHHHHHHH
28.3927732954
52PhosphorylationEVWHLLRTASLHLRG
HHHHHHHHHHHHHCC
22.1424719451
72UbiquitinationALQLHQQKERFPTQH
HHHHHHHHHCCCCHH
44.26-
172UbiquitinationVPGELLQKLRFGSQI
CCHHHHHHHHHCCEE
41.412190698
177PhosphorylationLQKLRFGSQIFIEHV
HHHHHHCCEEEEEEE
19.86-
189PhosphorylationEHVADVDTLLECVNK
EEECCHHHHHHHHHC
32.84-
196UbiquitinationTLLECVNKKVPVLLS
HHHHHHHCCCCHHHH
34.45-
197UbiquitinationLLECVNKKVPVLLSR
HHHHHHCCCCHHHHC
46.71-
225PhosphorylationPFRCEFDSQASAPRA
CEECCCCCCCCCCHH
32.7317525332
241PhosphorylationHLQSLGATLRELSSA
HHHHHHHHHHHHHHH
25.26-

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
225SPhosphorylationKinaseATMQ13315
PSP
225SPhosphorylationKinaseATRQ13535
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XRCC3_HUMAN !!

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 XRCC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RA51C_HUMANRAD51Cphysical
11331762
ZNHI3_HUMANZNHIT3physical
20211142
FANCG_HUMANFANCGphysical
20450923
FANCG_HUMANFANCGphysical
18212739
FANCG_HUMANFANCGphysical
16621732
SWAP1_HUMANSWSAP1physical
21965664
BAP1_HUMANBAP1physical
25640309
BCAS3_HUMANBCAS3physical
25640309
GROA_HUMANCXCL1physical
25640309
FA84B_HUMANFAM84Bphysical
25640309
GREB1_HUMANGREB1physical
25640309
ITIH5_HUMANITIH5physical
25640309
MRC2_HUMANMRC2physical
25640309
OSGI1_HUMANOSGIN1physical
25640309
HOP2_HUMANPSMC3IPphysical
25640309
BRE1A_HUMANRNF20physical
25640309
SG3A1_HUMANSCGB3A1physical
25640309
SPB5_HUMANSERPINB5physical
25640309
SNAI1_HUMANSNAI1physical
25640309
TFF1_HUMANTFF1physical
25640309
TRI25_HUMANTRIM25physical
25640309
DSRAD_HUMANADARphysical
26496610
A4_HUMANAPPphysical
26496610
AT2A2_HUMANATP2A2physical
26496610
ATPA_HUMANATP5A1physical
26496610
BRCA2_HUMANBRCA2physical
26496610
CALU_HUMANCALUphysical
26496610
TCPZ_HUMANCCT6Aphysical
26496610
CDK9_HUMANCDK9physical
26496610
CLCN7_HUMANCLCN7physical
26496610
COPA_HUMANCOPAphysical
26496610
CPSM_HUMANCPS1physical
26496610
TIM8A_HUMANTIMM8Aphysical
26496610
SYFA_HUMANFARSAphysical
26496610
FKBP5_HUMANFKBP5physical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
DNJA1_HUMANDNAJA1physical
26496610
HS90B_HUMANHSP90AB1physical
26496610
CH60_HUMANHSPD1physical
26496610
IMDH1_HUMANIMPDH1physical
26496610
IMDH2_HUMANIMPDH2physical
26496610
TNPO1_HUMANTNPO1physical
26496610
KTN1_HUMANKTN1physical
26496610
METH_HUMANMTRphysical
26496610
OPA1_HUMANOPA1physical
26496610
PYC_HUMANPCphysical
26496610
PMS2_HUMANPMS2physical
26496610
DPOLB_HUMANPOLBphysical
26496610
PP1RA_HUMANPPP1R10physical
26496610
SYQ_HUMANQARSphysical
26496610
RA51C_HUMANRAD51Cphysical
26496610
RCN1_HUMANRCN1physical
26496610
RNF5_HUMANRNF5physical
26496610
RL10_HUMANRPL10physical
26496610
AAAT_HUMANSLC1A5physical
26496610
RU17_HUMANSNRNP70physical
26496610
SSRG_HUMANSSR3physical
26496610
TAP1_HUMANTAP1physical
26496610
TCPA_HUMANTCP1physical
26496610
LAP2A_HUMANTMPOphysical
26496610
LAP2B_HUMANTMPOphysical
26496610
ENPL_HUMANHSP90B1physical
26496610
TCPG_HUMANCCT3physical
26496610
NCOA4_HUMANNCOA4physical
26496610
RBM10_HUMANRBM10physical
26496610
EIF3A_HUMANEIF3Aphysical
26496610
EIF3F_HUMANEIF3Fphysical
26496610
RIOK3_HUMANRIOK3physical
26496610
EI2BD_HUMANEIF2B4physical
26496610
ZW10_HUMANZW10physical
26496610
MED17_HUMANMED17physical
26496610
TECR_HUMANTECRphysical
26496610
IF2P_HUMANEIF5Bphysical
26496610
NUP93_HUMANNUP93physical
26496610
MED24_HUMANMED24physical
26496610
ZC11A_HUMANZC3H11Aphysical
26496610
MED16_HUMANMED16physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
CMC2_HUMANSLC25A13physical
26496610
RBM5_HUMANRBM5physical
26496610
SF3A1_HUMANSF3A1physical
26496610
CEPT1_HUMANCEPT1physical
26496610
HAX1_HUMANHAX1physical
26496610
CHERP_HUMANCHERPphysical
26496610
ERLN1_HUMANERLIN1physical
26496610
TCPQ_HUMANCCT8physical
26496610
STIP1_HUMANSTIP1physical
26496610
CKAP4_HUMANCKAP4physical
26496610
GCN1_HUMANGCN1L1physical
26496610
SF3B2_HUMANSF3B2physical
26496610
COPE_HUMANCOPEphysical
26496610
GPN1_HUMANGPN1physical
26496610
PHB2_HUMANPHB2physical
26496610
DNJC8_HUMANDNAJC8physical
26496610
CNDD3_HUMANNCAPD3physical
26496610
UBR4_HUMANUBR4physical
26496610
SF3B1_HUMANSF3B1physical
26496610
FKBP8_HUMANFKBP8physical
26496610
LTN1_HUMANLTN1physical
26496610
ERAL1_HUMANERAL1physical
26496610
MYOF_HUMANMYOFphysical
26496610
TIM13_HUMANTIMM13physical
26496610
QCR8_HUMANUQCRQphysical
26496610
SO4A1_HUMANSLCO4A1physical
26496610
HOOK2_HUMANHOOK2physical
26496610
PI3R4_HUMANPIK3R4physical
26496610
UBR5_HUMANUBR5physical
26496610
EXOC6_HUMANEXOC6physical
26496610
AGGF1_HUMANAGGF1physical
26496610
IPO9_HUMANIPO9physical
26496610
CCAR1_HUMANCCAR1physical
26496610
UN45A_HUMANUNC45Aphysical
26496610
ERBIN_HUMANERBB2IPphysical
26496610
JPH1_HUMANJPH1physical
26496610
NCLN_HUMANNCLNphysical
26496610
TOM22_HUMANTOMM22physical
26496610
PCNP_HUMANPCNPphysical
26496610
RCN3_HUMANRCN3physical
26496610
SQOR_HUMANSQRDLphysical
26496610
CTF18_HUMANCHTF18physical
26496610
MMS19_HUMANMMS19physical
26496610
SPA5L_HUMANSPATA5L1physical
26496610
DERL1_HUMANDERL1physical
26496610
GEMI7_HUMANGEMIN7physical
26496610
SFXN3_HUMANSFXN3physical
26496610
BACD3_HUMANKCTD10physical
26496610
NSRP1_HUMANNSRP1physical
26496610
HDGR2_HUMANHDGFRP2physical
26496610
SPF45_HUMANRBM17physical
26496610
PPIL4_HUMANPPIL4physical
26496610
TB182_HUMANTNKS1BP1physical
26496610
ZN598_HUMANZNF598physical
26496610
SFXN1_HUMANSFXN1physical
26496610
CC124_HUMANCCDC124physical
26496610
ADIP_HUMANSSX2IPphysical
26496610
BAP18_HUMANC17orf49physical
26496610
FANCA_HUMANFANCAphysical
28215707

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114480Breast cancer (BC)
613972Melanoma, cutaneous malignant 6 (CMM6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XRCC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-225, AND MASSSPECTROMETRY.

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