RFA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RFA1_MOUSE
• UniProt AC: Q8VEE4
• Protein Name: Replication protein A 70 kDa DNA-binding subunit
• Gene Name: Rpa1
• Organism: Mus musculus (Mouse).
• Sequence Length: 623
• Subcellular Localization: Nucleus . Nucleus, PML body .
• Protein Description: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance..
• Protein Sequence: MVGHLSEGAIEVMIQQENTSIKPILQVINIRPISTGNRSPRYRLLMSDGLNTLSSFMLATQLNTLVEGGQLASNCVCQVHKFIVNTLKDGRKVVVLMDLEVMKSAEDVGLKIGNPVPYNEGYGQQQQQQQQQQQQAVPSPASAATPPASKPQPQNGSLGMGSTAAKAYGASKPFGKPAGTGLLQPSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGALKIANKQFSAVKNDYEMTFNNETSVLPCEDGHHLPTVQFDFTGIGDLESKAKDALVDIIGICKSYEDSIKITVKSNNREVAKRNIYLMDMSGKVVTTTLWGEDADKFDGSRQPVMAIKGARVSDFGGRSLSVLSSSTVIVNPDIPEAYKLRGWFDSEGQALDGVSISDHRSGGAGGGNTNWKTLHEAKSENLGQGDKADYFSTVAAVVFLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDREFPNFKYRMILSANIADFQENQWVTCFQESAEAILGQNTMYLGELKEKNEQAFEEVFQNANFRSFTFRIRVKLETYNDESRIKATVMDVKPVDFRDYGRRLIANIRKNM

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
1	Acetylation	-------MVGHLSEG -------CCCCCCCC	8.01	-
34	Phosphorylation	VINIRPISTGNRSPR EEECEECCCCCCCHH	32.70	26643407
35	Phosphorylation	INIRPISTGNRSPRY EECEECCCCCCCHHH	38.91	28066266
39	Phosphorylation	PISTGNRSPRYRLLM ECCCCCCCHHHEEEC	20.10	28066266
88	Ubiquitination	KFIVNTLKDGRKVVV HHHHCCCCCCCEEEE	56.98	-
172	Acetylation	AKAYGASKPFGKPAG HHHHCCCCCCCCCCC	43.78	23806337
176	Acetylation	GASKPFGKPAGTGLL CCCCCCCCCCCCCCC	31.88	23806337
186	Phosphorylation	GTGLLQPSGGTQSKV CCCCCCCCCCCCCCE	36.57	27841257
189	Phosphorylation	LLQPSGGTQSKVVPI CCCCCCCCCCCEEEE	32.94	-
198	Phosphorylation	SKVVPIASLTPYQSK CCEEEECCCCCCCCC	33.23	28066266
200	Phosphorylation	VVPIASLTPYQSKWT EEEECCCCCCCCCCE	19.91	28066266
202	Phosphorylation	PIASLTPYQSKWTIC EECCCCCCCCCCEEE	21.86	28066266
204	Phosphorylation	ASLTPYQSKWTICAR CCCCCCCCCCEEEEE	25.07	28066266
268	Acetylation	NKVYYFSKGALKIAN CEEEEECHHHHHHHC	38.00	-
380	Phosphorylation	DADKFDGSRQPVMAI CHHCCCCCCCCEEEE	29.59	-
393	Phosphorylation	AIKGARVSDFGGRSL EEECCEECCCCCCEE	22.97	25266776
399	Phosphorylation	VSDFGGRSLSVLSSS ECCCCCCEEEEEECC	28.42	27600695
401	Phosphorylation	DFGGRSLSVLSSSTV CCCCCEEEEEECCEE	23.43	27600695
407	Phosphorylation	LSVLSSSTVIVNPDI EEEEECCEEEECCCC	19.05	26239621
418	Phosphorylation	NPDIPEAYKLRGWFD CCCCCHHHHHCCCCC	14.64	25367039
467	Ubiquitination	ENLGQGDKADYFSTV CCCCCCCHHHHHHHH	50.40	-
470	Phosphorylation	GQGDKADYFSTVAAV CCCCHHHHHHHHHHH	12.32	-
498	Ubiquitination	PTQDCNKKVIDQQNG CCCCCCCHHHHCCCC	30.36	-
562	Ubiquitination	YLGELKEKNEQAFEE EHHHHHHHHHHHHHH	65.28	-
594	Phosphorylation	LETYNDESRIKATVM EEECCCCCCEEEEEE	42.01	27357545
604	Ubiquitination	KATVMDVKPVDFRDY EEEEECCCCCCHHHH	34.75	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RFA1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
458	K	Sumoylation	Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site.	-
586	K	Sumoylation	Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RFA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIPIN_MOUSE	Tipin	physical	17141802
TIM_MOUSE	Timeless	physical	17141802

Drug and Disease Associations

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