RA51C_HUMAN - dbPTM
RA51C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RA51C_HUMAN
UniProt AC O43502
Protein Name DNA repair protein RAD51 homolog 3
Gene Name RAD51C
Organism Homo sapiens (Human).
Sequence Length 376
Subcellular Localization Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at
Protein Description Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD21 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) 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. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis..
Protein Sequence MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSESHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVIVDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRKQRLATLYKSPSQKECTVLFQIKPQGFRDTVVTSACSLQTEGSLSTRKRSRDPEEEL
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
16PhosphorylationEMQRDLVSFPLSPAV
EEEHHHHCCCCCHHH
28.5730266825
20PhosphorylationDLVSFPLSPAVRVKL
HHHCCCCCHHHHHEE
15.8530266825
26UbiquitinationLSPAVRVKLVSAGFQ
CCHHHHHEEEECCCC
32.3821906983
42UbiquitinationAEELLEVKPSELSKE
HHHHHCCCHHHHHHH
33.1921906983
42SumoylationAEELLEVKPSELSKE
HHHHHCCCHHHHHHH
33.19-
48UbiquitinationVKPSELSKEVGISKA
CCHHHHHHHHCCCHH
69.8821906983
54UbiquitinationSKEVGISKAEALETL
HHHHCCCHHHHHHHH
48.6121906983
60O-linked_GlycosylationSKAEALETLQIIRRE
CHHHHHHHHHHHHHH
25.4729237092
72UbiquitinationRRECLTNKPRYAGTS
HHHHHHCCCCCCCCC
26.1527667366
72AcetylationRRECLTNKPRYAGTS
HHHHHHCCCCCCCCC
26.1525953088
83UbiquitinationAGTSESHKKCTALEL
CCCCHHHHCCHHHHH
59.8427667366
84UbiquitinationGTSESHKKCTALELL
CCCHHHHCCHHHHHH
31.2422817900
131 (in isoform 2)Ubiquitination-30.59-
211UbiquitinationILSHIYYFRCRDYTE
HHHHHHHHCCCCHHH
3.1422817900
212UbiquitinationLSHIYYFRCRDYTEL
HHHHHHHCCCCHHHH
9.8422817900
216UbiquitinationYYFRCRDYTELLAQV
HHHCCCCHHHHHHHH
5.2422817900
217UbiquitinationYFRCRDYTELLAQVY
HHCCCCHHHHHHHHH
25.1722817900
256PhosphorylationRHDLDDLSLRTRLLN
CCCCCCHHHHHHHHH
23.8524719451
304PhosphorylationLVPALGESWGHAATI
EEECCCCCCCHHHHE
36.2429083192
310PhosphorylationESWGHAATIRLIFHW
CCCCHHHHEEHEEEC
13.8629083192
328UbiquitinationQRLATLYKSPSQKEC
HHHHHHCCCCCCCEE
60.0322817900
329UbiquitinationRLATLYKSPSQKECT
HHHHHCCCCCCCEEE
19.0722817900
333UbiquitinationLYKSPSQKECTVLFQ
HCCCCCCCEEEEEEE
60.1233845483
334UbiquitinationYKSPSQKECTVLFQI
CCCCCCCEEEEEEEE
27.9922817900
342UbiquitinationCTVLFQIKPQGFRDT
EEEEEEECCCCCCCE
22.09-
369PhosphorylationSLSTRKRSRDPEEEL
CCCCCCCCCCCHHCC
44.0325690035

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

Oops, there are no upstream regulatory protein records of RA51C_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RA51C_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 RA51C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RA51B_HUMANRAD51Bphysical
15115758
XRCC3_HUMANXRCC3physical
15115758
XRCC2_HUMANXRCC2physical
11744692
XRCC3_HUMANXRCC3physical
11744692
RA51B_HUMANRAD51Bphysical
11744692
RA51D_HUMANRAD51Dphysical
11744692
XRCC3_HUMANXRCC3physical
11842113
RA51D_HUMANRAD51Dphysical
11842113
XRCC2_HUMANXRCC2physical
11842113
RAD51_HUMANRAD51physical
16395335
A4_HUMANAPPphysical
21832049
SWAP1_HUMANSWSAP1physical
21965664
RA51D_HUMANRAD51Dphysical
27161866
KLH10_HUMANKLHL10physical
28514442
PTN9_HUMANPTPN9physical
28514442
CC140_HUMANCCDC140physical
28514442
HELQ_HUMANHELQphysical
24005329
RAD51_HUMANRAD51physical
24141787
RA51B_HUMANRAD51Bphysical
24141787
RA51D_HUMANRAD51Dphysical
24141787
PALB2_HUMANPALB2physical
24141787
BRCA2_HUMANBRCA2physical
24141787
XRCC2_HUMANXRCC2physical
24141787
XRCC3_HUMANXRCC3physical
24141787

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613390Fanconi anemia complementation group O (FANCO)
613399Breast-ovarian cancer, familial, 3 (BROVCA3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RA51C_HUMAN

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Related Literatures of Post-Translational Modification

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