dbPTM

RAD51_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAD51_HUMAN
UniProt AC	Q06609
Protein Name	DNA repair protein RAD51 homolog 1
Gene Name	RAD51
Organism	Homo sapiens (Human).
Sequence Length	339
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasm, perinuclear region. Mitochondrion matrix . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage indu
Protein Description	Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). [PubMed: 28575658 Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange]
Protein Sequence	MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAMQMQLEA ------CCCCEEEEC	9.27	22814378
13	Phosphorylation	QLEANADTSVEEESF EEECCCCCCCCHHHC	32.06	26074081
14	Phosphorylation	LEANADTSVEEESFG EECCCCCCCCHHHCC	28.25	26074081
39	Ubiquitination	GINANDVKKLEEAGF CCCHHHHHHHHHCCC	55.28	32015554
48	Phosphorylation	LEEAGFHTVEAVAYA HHHCCCEEEEEEEEC	20.13	26437602
54	Phosphorylation	HTVEAVAYAPKKELI EEEEEEEECCHHHHE	19.48	9461559
57	Ubiquitination	EAVAYAPKKELINIK EEEEECCHHHHEECC	51.19	22817900
58 (in isoform 4)	Ubiquitination	-	57.61	-
58	Ubiquitination	AVAYAPKKELINIKG EEEECCHHHHEECCC	57.61	21890473
58 (in isoform 1)	Ubiquitination	-	57.61	21890473
58 (in isoform 2)	Ubiquitination	-	57.61	21890473
58	Ubiquitination	AVAYAPKKELINIKG EEEECCHHHHEECCC	57.61	21890473
58	Ubiquitination	AVAYAPKKELINIKG EEEECCHHHHEECCC	57.61	22817900
64 (in isoform 1)	Ubiquitination	-	45.78	21890473
64	Ubiquitination	KKELINIKGISEAKA HHHHEECCCCCHHHH	45.78	21890473
64 (in isoform 2)	Ubiquitination	-	45.78	21890473
64 (in isoform 4)	Ubiquitination	-	45.78	-
64	Ubiquitination	KKELINIKGISEAKA HHHHEECCCCCHHHH	45.78	21890473
64	Ubiquitination	KKELINIKGISEAKA HHHHEECCCCCHHHH	45.78	27667366
73	Ubiquitination	ISEAKADKILAEAAK CCHHHHHHHHHHHHH	44.47	29967540
95 (in isoform 4)	Phosphorylation	-	35.21	24719451
95	Phosphorylation	TATEFHQRRSEIIQI HHHHHHHHHHHCEEE	35.21	24719451
99 (in isoform 4)	Phosphorylation	-	2.71	22210691
101 (in isoform 4)	Phosphorylation	-	32.41	22210691
107 (in isoform 1)	Ubiquitination	-	64.74	21890473
107	Ubiquitination	IQITTGSKELDKLLQ EEEECCCHHHHHHHH	64.74	21906983
120 (in isoform 4)	Phosphorylation	-	12.31	22210691
156 (in isoform 1)	Ubiquitination	-	26.19	21890473
156	Ubiquitination	DRGGGEGKAMYIDTE CCCCCCCEEEEECCC	26.19	2190698
157 (in isoform 4)	Ubiquitination	-	13.58	-
301	Phosphorylation	HASTTRLYLRKGRGE EECCCEEEEECCCCC	10.94	-
309	Phosphorylation	LRKGRGETRICKIYD EECCCCCCEEEEEEC	28.32	12442171
315	Phosphorylation	ETRICKIYDSPCLPE CCEEEEEECCCCCCH	8.89	10212258
317	Phosphorylation	RICKIYDSPCLPEAE EEEEEECCCCCCHHH	10.67	22210691

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
13	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
14	S	Phosphorylation	Kinase	PLK1	P53350	PSP
54	Y	Phosphorylation	Kinase	ABL	P00519	PSP
54	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
309	T	Phosphorylation	Kinase	CHEK1	O14757	Uniprot
315	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
315	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
315	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBH1	Q8NFZ0	PMID:25585578

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
309	T	Phosphorylation		15665856
Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination.

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 RAD51_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
R51A1_HUMAN	RAD51AP1	physical	9396801
EIF2D_HUMAN	EIF2D	physical	17353931
CAB39_HUMAN	CAB39	physical	17353931
TIM13_HUMAN	TIMM13	physical	17353931
P53_HUMAN	TP53	physical	14636569
RAD52_HUMAN	RAD52	physical	10212258
BLM_HUMAN	BLM	physical	11278509
RAD51_HUMAN	RAD51	physical	12442171
RA51B_HUMAN	RAD51B	physical	15065660
RA51C_HUMAN	RAD51C	physical	15065660
RA51D_HUMAN	RAD51D	physical	15065660
XRCC2_HUMAN	XRCC2	physical	15065660
XRCC3_HUMAN	XRCC3	physical	15065660
ABL1_HUMAN	ABL1	physical	10212258
ATM_HUMAN	ATM	physical	10212258
RAD51_HUMAN	RAD51	physical	14580352
VIME_HUMAN	VIM	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
FSBP_HUMAN	RAD54B	physical	10851248
RA54B_HUMAN	RAD54B	physical	10851248
RAD51_HUMAN	RAD51	physical	10851248
DMC1_HUMAN	DMC1	physical	10562567
P53_HUMAN	TP53	physical	8617246
BRCA2_HUMAN	BRCA2	physical	9126738
DNJA3_HUMAN	DNAJA3	physical	11005857
SUMO1_HUMAN	SUMO1	physical	8812453
ATRX_HUMAN	ATRX	physical	12205100
UBC9_HUMAN	UBE2I	physical	8610150
RAD51_HUMAN	RAD51	physical	8610150
RFA1_HUMAN	RPA1	physical	12077133
UBC9_HUMAN	UBE2I	physical	8921390
RAD18_HUMAN	RAD18	physical	19396164
MCPH1_HUMAN	MCPH1	physical	20107607
MCPH1_HUMAN	MCPH1	physical	19549900
MDC1_HUMAN	MDC1	physical	16186822
WRN_HUMAN	WRN	physical	17118963
RAD52_HUMAN	RAD52	physical	17118963
MSH2_HUMAN	MSH2	physical	15064730
MSH6_HUMAN	MSH6	physical	15064730
BLM_HUMAN	BLM	physical	15064730
P53_HUMAN	TP53	physical	15064730
ATRX_HUMAN	ATRX	physical	19671661
PML_HUMAN	PML	physical	21998700
BRCA1_HUMAN	BRCA1	physical	9008167
BRCA2_HUMAN	BRCA2	physical	10551859
BRCA2_HUMAN	BRCA2	physical	15800615
CHK1_HUMAN	CHEK1	physical	15665856
DMC1_HUMAN	DMC1	physical	17541404
BRCA2_HUMAN	BRCA2	physical	17541404
FSBP_HUMAN	RAD54B	physical	16428451
RA54B_HUMAN	RAD54B	physical	16428451
RFA1_HUMAN	RPA1	physical	19338310
UGDH_HUMAN	UGDH	physical	21988832
ROA2_HUMAN	HNRNPA2B1	physical	22863883
SWAP1_HUMAN	SWSAP1	physical	21965664
CAD13_HUMAN	CDH13	physical	25640309
CYTM_HUMAN	CST6	physical	25640309
FA84B_HUMAN	FAM84B	physical	25640309
IL24_HUMAN	IL24	physical	25640309
ITIH5_HUMAN	ITIH5	physical	25640309
ARY2_HUMAN	NAT2	physical	25640309
ST14_HUMAN	ST14	physical	25640309
TFF1_HUMAN	TFF1	physical	25640309
NSD3_HUMAN	WHSC1L1	physical	25640309
NELFB_HUMAN	NELFB	physical	25640309
CSK2B_HUMAN	CSNK2B	physical	25640309
HS90A_HUMAN	HSP90AA1	physical	25640309
JIP3_HUMAN	MAPK8IP3	physical	25640309
PCSK1_HUMAN	PCSK1N	physical	25640309
SIR2_HUMAN	SIRT2	physical	25640309
UMPS_HUMAN	UMPS	physical	25640309
UBP10_HUMAN	USP10	physical	25640309
CASP3_HUMAN	CASP3	physical	25241761
TBG1_HUMAN	TUBG1	physical	25499220
BRCA1_HUMAN	BRCA1	physical	25499220
ESR1_HUMAN	ESR1	physical	25499220
RAD18_HUMAN	RAD18	physical	25893307
BRCA2_HUMAN	BRCA2	physical	26145171
BRCA2_HUMAN	BRCA2	physical	25585578
ERCC5_HUMAN	ERCC5	physical	26833090
BRCA2_HUMAN	BRCA2	physical	26833090
PALB2_HUMAN	PALB2	physical	26833090
SEM1_HUMAN	SHFM1	physical	26833090
UCHL3_HUMAN	UCHL3	physical	27941124
BRCA2_HUMAN	BRCA2	physical	27941124
PARI_HUMAN	PARPBP	physical	22153967
TBA1A_HUMAN	TUBA1A	physical	28613254
LMNB1_HUMAN	LMNB1	physical	28613254
FANCA_HUMAN	FANCA	physical	28215707
SPTA1_HUMAN	SPTA1	physical	16889989
BCR_HUMAN	BCR	physical	21653319
ABL1_HUMAN	ABL1	physical	21653319
RFWD3_HUMAN	RFWD3	physical	28575658
H2AX_HUMAN	H2AFX	physical	28190324

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114480	Breast cancer (BC)
614508	Mirror movements 2 (MRMV2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RAD51_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The cell-cycle checkpoint kinase Chk1 is required for mammalianhomologous recombination repair."; Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G.,Lundin C., Bartek J., Helleday T.; Nat. Cell Biol. 7:195-201(2005). Cited for: INTERACTION WITH CHEK1, SUBCELLULAR LOCATION, PHOSPHORYLATION ATTHR-309, AND MUTAGENESIS OF THR-309.	15665856 [Abstract]
"Regulation of Rad51 function by c-Abl in response to DNA damage."; Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T.,Kharbanda S., Wang R., Sung P., Shinohara A., Weichselbaum R.,Kufe D.; J. Biol. Chem. 273:3799-3802(1998). Cited for: INTERACTION WITH ABL1, AND PHOSPHORYLATION AT TYR-54.	9461559 [Abstract]

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