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Protein Page:
RFA2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RFA2 Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage. Heterotrimer of 70, 32 and 14 kDa chains (canonical replication protein A complex). Component of the alternative replication protein A complex (aRPA) composed of RPA1, RPA3 and RPA4. The DNA-binding activity may reside exclusively on the 70 kDa subunit. Binds to SERTAD3/RBT1. Interacts with TIPIN. Directly interacts with PPP4R2, but not with SMEK2; this interaction is DNA damage-dependent and leads RPA2 dephosphorylation by PPP4C recruitment. Interacts with RAD51, preferentially when hyperphosphorylated. Directly interacts with RFWD3. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA replication
Chromosomal Location of Human Ortholog: 1p35
Cellular Component: nucleoplasm; chromosome, telomeric region; PML body; DNA replication factor A complex; nucleolus; nucleus
Molecular Function: protein binding; enzyme binding; ubiquitin protein ligase binding; damaged DNA binding; protein N-terminus binding; protein phosphatase binding; single-stranded DNA binding
Biological Process: G1 DNA damage checkpoint; mismatch repair; DNA strand elongation during DNA replication; DNA repair; double-strand break repair via homologous recombination; telomere maintenance via semi-conservative replication; DNA recombinase assembly; base-excision repair; nucleotide-excision repair; double-strand break repair; transcription-coupled nucleotide-excision repair; telomere maintenance via recombination; nucleotide-excision repair, DNA damage removal; nucleotide-excision repair, DNA gap filling; mitotic cell cycle; DNA replication; telomere maintenance; G1/S transition of mitotic cell cycle
Reference #:  P15927 (UniProtKB)
Alt. Names/Synonyms: REPA2; Replication factor A protein 2; Replication protein A 32 kDa subunit; Replication protein A 34 kDa subunit; replication protein A2, 32kDa; RF-A protein 2; RFA2; RP-A p32; RP-A p34; RPA2; RPA32; RPA34
Gene Symbols: RPA2
Molecular weight: 29,247 Da
Basal Isoelectric point: 5.75  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RFA2

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: T21‑p, S33‑p
apoptosis, induced: S4‑p, S8‑p
cell cycle regulation: S4‑p, S8‑p, T21‑p, S23‑p, S29‑p, S33‑p
cell growth, altered: S4‑p, S8‑p, S11‑p, S12‑p, S13‑p, T21‑p, S33‑p
intracellular localization: S4‑p, S8‑p, S11‑p, S12‑p, S13‑p, T21‑p, S23‑p, S29‑p, S33‑p
phosphorylation: T21‑p, S33‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
19 1 S4-p ____MWNsGFEsyGs
20 1 S8-p MWNsGFEsyGsssyG
0 1 Y9-p WNsGFEsyGsssyGG
0 1 G10 NsGFEsyGsssyGGA
3 0 S11-p sGFEsyGsssyGGAG
3 1 S12-p GFEsyGsssyGGAGG
3 0 S13-p FEsyGsssyGGAGGY
0 2 Y14-p EsyGsssyGGAGGYt
13 0 T21-p yGGAGGYtQsPGGFG
6 1 S23-p GAGGYtQsPGGFGsP
8 2 S29-p QsPGGFGsPAPsQAE
0 1 A31 PGGFGsPAPsQAEKK
19 1 S33-p GFGsPAPsQAEKKSR
0 1 S39 PsQAEKKSRARAQHI
1 0 S52-p HIVPCTIsQLLSATL
1 0 S72-p RIGNVEIsQVTIVGI
0 3 K85-ub GIIRHAEkAPtNIVY
0 1 T88-p RHAEkAPtNIVYkID
0 1 K93-ub APtNIVYkIDDMTAA
0 4 K127-ub VPPETYVkVAGHLRS
0 1 K171-ub NAHMVLSkANsQPSA
1 0 S174-p MVLSkANsQPSAGRA
0 1 N232 LNFQDLKNQLkHMsV
0 1 K235-ub QDLKNQLkHMsVsSI
0 3 S238-p KNQLkHMsVsSIKQA
0 1 S240-p QLkHMsVsSIKQAVD
0 1 S241 LkHMsVsSIKQAVDF
  mouse

 
S4-p ____MWNsGFESFtS
S8 MWNsGFESFtSsTyG
F9 WNsGFESFtSsTyGG
T10-p NsGFESFtSsTyGGR
S11 sGFESFtSsTyGGRG
S12-p GFESFtSsTyGGRGG
T13 FESFtSsTyGGRGGY
Y14-p ESFtSsTyGGRGGYT
T21 yGGRGGYTQSPGGFG
S23 GRGGYTQSPGGFGsP
S29-p QSPGGFGsPtPsQAE
T31-p PGGFGsPtPsQAEKK
S33-p GFGsPtPsQAEKKsR
S39-p PsQAEKKsRVRAQHI
S52 HIVPCTISQLLSATL
S72 RIGDVEISQVTIVGI
K85 GIIRHAEKAPTNIVY
T88 RHAEKAPTNIVYKID
K93 APTNIVYKIDDMTAP
K127 VPPETYVKVAGHLRS
K171 NSHMMLSKPNSQASA
S174 MMLSKPNSQASAGRP
S232-p LNFQDLRsQLQHMPV
Q235 QDLRsQLQHMPVPsI
P238 RsQLQHMPVPsIKQA
P240 QLQHMPVPsIKQAVD
S241-p LQHMPVPsIKQAVDF
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