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Reviewed, UniProtKB/Swiss-Prot P15927 (RFA2_HUMAN)

Last modified March 2, 2010. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Replication protein A 32 kDa subunit

Short name=RP-A p32
Alternative name(s):
Replication protein A 34 kDa subunit
Short name=RP-A p34
Replication factor A protein 2
Short name=RF-A protein 2
Gene names
Name:RPA2
Synonyms:REPA2, RPA32, RPA34
OrganismHomo sapiens (Human) [Complete 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. Ref.9

Subunit structure

Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding activity may reside exclusively on the 70 kDa subunit. Binds to SERTAD3/RBT1. Interacts with TIPIN. Ref.7 Ref.10 Ref.11

Subcellular location

Nucleus. Note: Also present in PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA damage. Ref.8

Post-translational modification

Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). Phosphorylated by ATR upon DNA damage, which promotes its translocation to nuclear foci. Can be phosphorylated in vitro by PRKDC/DNA-PK in the presence of Ku and DNA, and by CDC2. Ref.8 Ref.6

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CREBBPQ927931EBI-621404,EBI-81215
GAPDHP044061EBI-621404,EBI-354056

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.12
Modified residue211Phosphothreonine; by PRKDC; in vitro Ref.6
Modified residue291Phosphoserine; by CDC2; in vitro Ref.6
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: dbSNP rs28988896. Ref.3
VAR_023300
Natural variant151G → R: dbSNP rs28988897. Ref.3
VAR_023301
Natural variant2031N → S: dbSNP rs28904899. Ref.3
VAR_023302

Experimental info

Mutagenesis291S → A: Reduces phosphorylation by CDC2. Ref.6

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.

Checksum: 680A88DB44410EBC
Show »

FASTA27830,156
Isoform 3.

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: 2406247] [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: 16710414] [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: 15489334] [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: 9139719] [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: 10982866] [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: 12814551] [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: 15205463] [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: 17141802] [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: 17296725] [Abstract]
Cited for: INTERACTION WITH TIPIN.
[12]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[13]"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: 10449415] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1 AND RPA3.
[14]"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: 11081631] [Abstract]
Cited for: STRUCTURE BY NMR OF 172-270.
[15]"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: 11927569] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171.
+Additional computationally mapped references.

Web resources

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.
IPIIPI00013939.
IPI00646500.
IPI00647667.
PIRA43711.
RefSeqNP_002937.1.
UniGeneHs.703070
Hs.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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-24187N.
IntActP15927. 24 interactions.
STRINGP15927.

PTM databases

PhosphoSiteP15927.

Proteomic databases

PRIDEP15927.

Genome annotation databases

EnsemblENST00000373912; ENSP00000363021; ENSG00000117748; Homo sapiens. [Genome view]
GeneID6118.
KEGGhsa:6118.
UCSCuc001bpd.1. human.
uc001bpe.1. human.

Organism-specific databases

CTD6118.
GeneCardsGC01M028090.
H-InvDBHIX0000302.
HGNCHGNC:10290. RPA2.
HPACAB016538.
MIM179836. gene.
PharmGKBPA34652.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07006.
HOVERGENHBG000086.
OMATHILEVI.
PhylomeDBP15927.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_216. DNA Repair.
REACT_383. DNA Replication.
REACT_7970. Telomere Maintenance.

Gene expression databases

ArrayExpressP15927.
BgeeP15927.
CleanExHS_RPA2.
GenevestigatorP15927.
GermOnlineENSG00000117748. Homo sapiens.

Family and domain databases

InterProIPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA_bd_OB_tRNA-helicase.
IPR014646. RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF08784. RPA_C. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PIRSFPIRSF036949. RPA32. 1 hit.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
ProtoNetSearch...

Other Resources

NextBio23759.
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: March 2, 2010
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents