P15927 (RFA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Replication protein A 32 kDa subunit
Short name=RP-A p32

Alternative name(s):
Replication factor A protein 2
Short name=RF-A protein 2
Replication protein A 34 kDa subunit
Short name=RP-A p34

Gene names

Name:	RPA2
Synonyms:	REPA2, RPA32, RPA34

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.13 Ref.14 Ref.15 Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange. Ref.9 Ref.13 Ref.14 Ref.15
Subunit structure	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. Ref.7 Ref.10 Ref.11 Ref.13 Ref.15 Ref.18 Ref.19
Subcellular location	Nucleus. Nucleus › PML body. Note: Also present in PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA damage. Ref.8 Ref.15 Ref.18 Ref.19
Post-translational modification	Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In response to DNA damage, recruited to DNA-repair nuclear foci, as a hypophosphorylated form. The necessary dephosphorylation step is catalyzed by PP4. Subsequent hyperphosphorylation, catalyzed by ATR, is required for RAD51 recruitment to chromatin and efficient DNA repair. Can be phosphorylated in vitro by PRKDC/DNA-PK in the presence of Ku and DNA, and by CDK1. Phosphorylation at Thr-21 depends upon RFWD3 presence. Ref.6 Ref.8 Ref.19

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombinase assembly Traceable author statement. Source: Reactome DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome regulation of double-strand break repair via homologous recombination Inferred from mutant phenotype Ref.15. Source: UniProtKB telomere maintenance via recombination Traceable author statement. Source: Reactome telomere maintenance via semi-conservative replication Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome
Cellular_component	DNA replication factor A complex Inferred from physical interaction PubMed 16135809. Source: MGI PML body Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	single-stranded DNA binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAPDH	P04406	2	EBI-621404,EBI-354056
RPA1	P27694	4	EBI-621404,EBI-621389
RPA3	P35244	3	EBI-621404,EBI-621428
XPA	P23025	3	EBI-621404,EBI-295222

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P15927-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P15927-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MWNS → MGRGDRNKRSIR

Note: No experimental confirmation available.

Isoform 3 (identifier: P15927-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MWNS → MWNSNDGGAG...QALILLFKTG

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

Replication protein A 32 kDa subunit

PRO_0000097270

Regions

Region

187 – 270

84

Interaction with TIPIN By similarity

Compositional bias

1 – 29

29

Gly/Ser-rich

Compositional bias

37 – 45

9

Arg/Lys-rich (basic)

Compositional bias

95 – 123

29

Asp/Glu-rich (acidic)

Compositional bias

127 – 145

19

Arg/Lys-rich (basic)

Compositional bias

247 – 270

24

Asp/Glu-rich (acidic)

Sites

Site

23

1

Not phosphorylated Probable

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6 Ref.16

Modified residue

21

1

Phosphothreonine; by PRKDC; in vitro Ref.6 Ref.19

Modified residue

23

1

Phosphoserine Ref.16

Modified residue

29

1

Phosphoserine; by CDK1; in vitro Ref.6 Ref.16

Modified residue

33

1

Phosphoserine; by PRKDC; in vitro Ref.6

Natural variations

Alternative sequence

1 – 4

4

MWNS → MGRGDRNKRSIR in isoform 2.

VSP_017201

Alternative sequence

1 – 4

4

MWNS → MWNSNDGGAGWRRKRIAGGF SKRASLGSERRVVAGEEGRE RSWGVWGSPAGRRRGRLGRL GQCLKGRSLREPAGFSEAWD VAQALILLFKTG in isoform 3.

VSP_017202

Natural variant

14

1

Y → S. Ref.3
Corresponds to variant rs28988896 [ dbSNP | Ensembl ].

VAR_023300

Natural variant

15

1

G → R. Ref.3
Corresponds to variant rs28988897 [ dbSNP | Ensembl ].

VAR_023301

Natural variant

203

1

N → S. Ref.3
Corresponds to variant rs28904899 [ dbSNP | Ensembl ].

VAR_023302

Experimental info

Mutagenesis

8

1

S → D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-33. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-23; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-23; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-23; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-23; D-29 and D-33. Ref.6 Ref.15

Mutagenesis

23

1

S → D: No effect on DNA synthesis following DNA damage; when associated with D-29. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-29 and D-33. Ref.15

Mutagenesis

29

1

S → A: Reduces phosphorylation by CDK1. Ref.6 Ref.15

Mutagenesis

29

1

S → D: No effect on DNA synthesis following DNA damage; when associated with D-23. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-33. Ref.6 Ref.15

Mutagenesis

33

1

S → D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-8. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-29. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-29. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-29. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-29. Ref.15

Secondary structure

1

.

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270

Helix Strand Turn

Details...

Beta strand

46 – 48

3

Helix

51 – 55

5

Beta strand

58 – 62

5

Beta strand

64 – 66

3

Beta strand

69 – 71

3

Beta strand

73 – 85

13

Beta strand

87 – 95

9

Beta strand

97 – 100

4

Beta strand

102 – 107

6

Beta strand

125 – 135

11

Beta strand

138 – 148

11

Helix

153 – 171

19

Helix

207 – 218

12

Turn

222 – 224

3

Helix

227 – 233

7

Helix

239 – 251

13

Beta strand

254 – 257

4

Beta strand

263 – 268

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 61A563EA7B34A9B1	FASTA	270	29,247
	10 20 30 40 50 60 MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV 70 80 90 100 110 120 DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV 130 140 150 160 170 180 PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR 190 200 210 220 230 240 APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS 250 260 270 SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE
	Isoform 2 [UniParc]. Checksum: 680A88DB44410EBC	FASTA	278	30,156
	10 20 30 40 50 60 MGRGDRNKRS IRGFESYGSS SYGGAGGYTQ SPGGFGSPAP SQAEKKSRAR AQHIVPCTIS 70 80 90 100 110 120 QLLSATLVDE VFRIGNVEIS QVTIVGIIRH AEKAPTNIVY KIDDMTAAPM DVRQWVDTDD 130 140 150 160 170 180 TSSENTVVPP ETYVKVAGHL RSFQNKKSLV AFKIMPLEDM NEFTTHILEV INAHMVLSKA 190 200 210 220 230 240 NSQPSAGRAP ISNPGMSEAG NFGGNSFMPA NGLTVAQNQV LNLIKACPRP EGLNFQDLKN 250 260 270 QLKHMSVSSI KQAVDFLSNE GHIYSTVDDD HFKSTDAE
	Isoform 3 [UniParc]. Checksum: B21291661BDEEAFA	FASTA	358	38,810
	10 20 30 40 50 60 MWNSNDGGAG WRRKRIAGGF SKRASLGSER RVVAGEEGRE RSWGVWGSPA GRRRGRLGRL 70 80 90 100 110 120 GQCLKGRSLR EPAGFSEAWD VAQALILLFK TGGFESYGSS SYGGAGGYTQ SPGGFGSPAP 130 140 150 160 170 180 SQAEKKSRAR AQHIVPCTIS QLLSATLVDE VFRIGNVEIS QVTIVGIIRH AEKAPTNIVY 190 200 210 220 230 240 KIDDMTAAPM DVRQWVDTDD TSSENTVVPP ETYVKVAGHL RSFQNKKSLV AFKIMPLEDM 250 260 270 280 290 300 NEFTTHILEV INAHMVLSKA NSQPSAGRAP ISNPGMSEAG NFGGNSFMPA NGLTVAQNQV 310 320 330 340 350 LNLIKACPRP EGLNFQDLKN QLKHMSVSSI KQAVDFLSNE GHIYSTVDDD HFKSTDAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of the 32-kDa subunit of human replication protein A." Erdile L.F., Wold M.S., Kelly T.J. J. Biol. Chem. 265:3177-3182(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	NIEHS SNPs program Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-14; ARG-15 AND SER-203.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney, Lung and Muscle.
[6]	"Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro." Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P., Hurwitz J. J. Biol. Chem. 272:12634-12641(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT MET-1, PHOSPHORYLATION AT THR-21; SER-29 AND SER-33, MASS SPECTROMETRY, MUTAGENESIS OF SER-29.
[7]	"RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A." Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S., Alaoui-Jamali M.A. Nucleic Acids Res. 28:3478-3485(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SERTAD3.
[8]	"ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation." Barr S.M., Leung C.G., Chang E.E., Cimprich K.A. Curr. Biol. 13:1047-1051(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[9]	"Coordinated regulation of replication protein A activities by its subunits p14 and p32." Weisshart K., Pestryakov P., Smith R.W.P., Hartmann H., Kremmer E., Lavrik O., Nasheuer H.-P. J. Biol. Chem. 279:35368-35376(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors." Gotter A.L., Suppa C., Emanuel B.S. J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIPIN.
[11]	"The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement." Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P., Cordeiro-Stone M., Sancar A., Kaufmann W.K. Mol. Cell. Biol. 27:3131-3142(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIPIN.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"An alternative form of replication protein a prevents viral replication in vitro." Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F., Wold M.S. J. Biol. Chem. 284:5324-5331(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ARPA COMPLEX, FUNCTION OF THE ARPA COMPLEX.
[14]	"An alternative form of replication protein a expressed in normal human tissues supports DNA repair." Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J., Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S. J. Biol. Chem. 285:4788-4797(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE ARPA COMPLEX.
[15]	"A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination." Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D. Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPP4C; PPP4R2 AND RAD51, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-8; SER-23; SER-29 AND SER-33.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"E3 ligase RFWD3 participates in replication checkpoint control." Gong Z., Chen J. J. Biol. Chem. 286:22308-22313(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RFWD3, SUBCELLULAR LOCATION.
[19]	"RING finger and WD repeat domain 3 (RFWD3) associates with replication protein A (RPA) and facilitates RPA-mediated DNA damage response." Liu S., Chu J., Yucer N., Leng M., Wang S.Y., Chen B.P., Hittelman W.N., Wang Y. J. Biol. Chem. 286:22314-22322(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RFWD3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-21.
[20]	"The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding." Bochkarev A., Bochkareva E., Frappier L., Edwards A.M. EMBO J. 18:4498-4504(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1 AND RPA3.
[21]	"Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA." Mer G., Bochkarev A., Gupta R., Bochkareva E., Frappier L., Ingles C.J., Edwards A.M., Chazin W.J. Cell 103:449-456(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 172-270.
[22]	"Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA." Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A. EMBO J. 21:1855-1863(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05249 mRNA. Translation: AAA36560.1.
CR450348 mRNA. Translation: CAG29344.1.
DQ001128 Genomic DNA. Translation: AAX84514.1.
AL109927 Genomic DNA. Translation: CAI21777.1.
AL109927 Genomic DNA. Translation: CAI21778.1.
AL109927 Genomic DNA. Translation: CAI21775.1.
BC001630 mRNA. Translation: AAH01630.1.
BC012157 mRNA. Translation: AAH12157.1.
BC021257 mRNA. Translation: AAH21257.1.

IPI

IPI00013939.
IPI00646500.
IPI00647667.

PIR

A43711.

RefSeq

NP_002937.1. NM_002946.3.

UniGene

Hs.79411.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DPU	NMR	-	A	172-270	[»]
1L1O	X-ray	2.80	B/E	44-171	[»]
1QUQ	X-ray	2.50	A/C	43-171	[»]
1Z1D	NMR	-	A	172-270	[»]
2PI2	X-ray	2.00	A/B/C/D	1-270	[»]
2PQA	X-ray	2.50	A/C	42-172	[»]
2Z6K	X-ray	3.00	A/B	1-270	[»]
3KDF	X-ray	1.98	B/D	42-172	[»]

ProteinModelPortal

P15927.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24187N.

IntAct

P15927. 42 interactions.

MINT

MINT-5002459.

STRING

9606.ENSP00000363021.

PTM databases

PhosphoSite

P15927.

Polymorphism databases

DMDM

132474.

Proteomic databases

PaxDb

P15927.

PRIDE

P15927.

Protocols and materials databases

DNASU

6118.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313433; ENSP00000363015; ENSG00000117748.
ENST00000373909; ENSP00000363017; ENSG00000117748.
ENST00000373912; ENSP00000363021; ENSG00000117748.

GeneID

6118.

KEGG

hsa:6118.

UCSC

uc001bpe.1. human.

Organism-specific databases

CTD

6118.

GeneCards

GC01M028218.

HGNC

HGNC:10290. RPA2.

HPA

CAB016538.
HPA026306.
HPA026309.

MIM

179836. gene.

neXtProt

NX_P15927.

PharmGKB

PA34652.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5235.

HOGENOM

HOG000216562.

HOVERGEN

HBG000086.

KO

K10739.

OMA

GGNSFMP.

OrthoDB

EOG4WQ13T.

PhylomeDB

P15927.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P15927.

Bgee

P15927.

CleanEx

HS_RPA2.

Genevestigator

P15927.

GermOnline

ENSG00000117748. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
2.40.50.140. 1 hit.

InterPro

IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA-helicase.
IPR014646. RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF08784. RPA_C. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]

PIRSF

PIRSF036949. RPA32. 1 hit.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RPA2. human.

EvolutionaryTrace

P15927.

GenomeRNAi

6118.

NextBio

23759.

SOURCE

Search...

Entry information

Entry name

RFA2_HUMAN

Accession

Primary (citable) accession number: P15927
Secondary accession number(s): Q52II0, Q5TEI9, Q5TEJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.