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P15927 (RFA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence 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.14 Ref.15 Ref.16

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.14 Ref.15 Ref.16

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.14 Ref.16 Ref.19 Ref.20

Subcellular location

Nucleus. NucleusPML body. Note: Also present in PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA damage. Ref.8 Ref.16 Ref.19 Ref.20

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.20

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombinase assembly

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

DNA replication

Inferred from direct assay Ref.1. Source: UniProtKB

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

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.16. Source: UniProtKB

telomere maintenance

Traceable author statement. Source: Reactome

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_componentDNA replication factor A complex

Inferred from direct assay Ref.1. Source: UniProtKB

PML body

Inferred from direct assay Ref.8. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionprotein phosphatase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Replication protein A 32 kDa subunit
PRO_0000097270

Regions

Region187 – 27084Interaction with TIPIN By similarity
Compositional bias1 – 2929Gly/Ser-rich
Compositional bias37 – 459Arg/Lys-rich (basic)
Compositional bias95 – 12329Asp/Glu-rich (acidic)
Compositional bias127 – 14519Arg/Lys-rich (basic)
Compositional bias247 – 27024Asp/Glu-rich (acidic)

Sites

Site231Not phosphorylated Probable

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6 Ref.13 Ref.17
Modified residue211Phosphothreonine; by PRKDC; in vitro Ref.6 Ref.20
Modified residue231Phosphoserine Ref.17
Modified residue291Phosphoserine; by CDK1; in vitro Ref.6 Ref.17
Modified residue331Phosphoserine; by PRKDC; in vitro Ref.6

Natural variations

Alternative sequence1 – 44MWNS → MGRGDRNKRSIR in isoform 2.
VSP_017201
Alternative sequence1 – 44MWNS → MWNSNDGGAGWRRKRIAGGF SKRASLGSERRVVAGEEGRE RSWGVWGSPAGRRRGRLGRL GQCLKGRSLREPAGFSEAWD VAQALILLFKTG in isoform 3.
VSP_017202
Natural variant141Y → S. Ref.3
Corresponds to variant rs28988896 [ dbSNP | Ensembl ].
VAR_023300
Natural variant151G → R. Ref.3
Corresponds to variant rs28988897 [ dbSNP | Ensembl ].
VAR_023301
Natural variant2031N → S. Ref.3
Corresponds to variant rs28904899 [ dbSNP | Ensembl ].
VAR_023302

Experimental info

Mutagenesis81S → 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.16
Mutagenesis231S → 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.16
Mutagenesis291S → A: Reduces phosphorylation by CDK1. Ref.6 Ref.16
Mutagenesis291S → 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.16
Mutagenesis331S → 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.16

Secondary structure

..................................... 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 61A563EA7B34A9B1

FASTA27029,247
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 680A88DB44410EBC
Show »

FASTA27830,156
Isoform 3 [UniParc].

Checksum: B21291661BDEEAFA
Show »

FASTA35838,810

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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.
[16]"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.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.

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.
PIRA43711.
RefSeqNP_001273005.1. NM_001286076.1.
NP_002937.1. NM_002946.4.
XP_005246022.1. XM_005245965.1.
UniGeneHs.79411.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPUNMR-A172-270[»]
1L1OX-ray2.80B/E44-171[»]
1QUQX-ray2.50A/C43-171[»]
1Z1DNMR-A172-270[»]
2PI2X-ray2.00A/B/C/D1-270[»]
2PQAX-ray2.50A/C42-172[»]
2Z6KX-ray3.00A/B1-270[»]
3KDFX-ray1.98B/D42-172[»]
ProteinModelPortalP15927.
SMRP15927. Positions 44-170, 202-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112038. 103 interactions.
DIPDIP-24187N.
IntActP15927. 51 interactions.
MINTMINT-5002459.
STRING9606.ENSP00000363021.

PTM databases

PhosphoSiteP15927.

Polymorphism databases

DMDM132474.

Proteomic databases

PaxDbP15927.
PRIDEP15927.

Protocols and materials databases

DNASU6118.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313433; ENSP00000363015; ENSG00000117748. [P15927-3]
ENST00000373909; ENSP00000363017; ENSG00000117748. [P15927-2]
ENST00000373912; ENSP00000363021; ENSG00000117748. [P15927-1]
GeneID6118.
KEGGhsa:6118.
UCSCuc001bpe.1. human. [P15927-1]

Organism-specific databases

CTD6118.
GeneCardsGC01M028218.
HGNCHGNC:10290. RPA2.
HPACAB016538.
HPA026306.
HPA026309.
MIM179836. gene.
neXtProtNX_P15927.
PharmGKBPA34652.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5235.
HOGENOMHOG000216562.
HOVERGENHBG000086.
KOK10739.
OMASNPGMGE.
OrthoDBEOG76X615.
PhylomeDBP15927.
TreeFamTF105242.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP15927.
BgeeP15927.
CleanExHS_RPA2.
GenevestigatorP15927.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
IPR014646. RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF08784. RPA_C. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PIRSFPIRSF036949. RPA32. 1 hit.
SUPFAMSSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRPA2. human.
EvolutionaryTraceP15927.
GeneWikiRPA2.
GenomeRNAi6118.
NextBio23759.
PROP15927.
SOURCESearch...

Entry information

Entry nameRFA2_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM