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P35244 (RFA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Replication protein A 14 kDa subunit

Short name=RP-A p14
Alternative name(s):
Replication factor A protein 3
Short name=RF-A protein 3
Gene names
Name:RPA3
Synonyms:REPA3, RPA14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.8 Ref.9

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.8 Ref.9

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. Interacts with RPA4. Ref.6 Ref.8

Subcellular location

Nucleus.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombinase assembly

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

DNA replication

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

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

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

Traceable author statement Ref.1. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionsingle-stranded DNA binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 121120Replication protein A 14 kDa subunit
PRO_0000097276

Amino acid modifications

Modified residue21N-acetylvaline Ref.7 Ref.11 Ref.12

Secondary structure

....................... 121
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35244 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 3FD99851959FB498

FASTA12113,569
        10         20         30         40         50         60 
MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN GTIELMEPLD 

        70         80         90        100        110        120 
EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN EAVKIIHDFP QFYPLGIVQH 


D 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A."
Umbricht C.B., Kelly T.J.
J. Biol. Chem. 268:6131-6138(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [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].
Tissue: Kidney and Lung.
[6]"Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex."
Keshav K.F., Chen C., Dutta A.
Mol. Cell. Biol. 15:3119-3128(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPA4.
[7]"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 VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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.
[9]"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.
[10]"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].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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) IN COMPLEX WITH RPA1 AND RPA2.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07493 mRNA. Translation: AAA58350.1.
BT007320 mRNA. Translation: AAP35984.1.
DQ003136 Genomic DNA. Translation: AAX84517.1.
AC004948 Genomic DNA. Translation: AAQ96878.1.
BC005264 mRNA. Translation: AAH05264.1.
BC009868 mRNA. Translation: AAH09868.1.
PIRA46008.
RefSeqNP_002938.1. NM_002947.3.
UniGeneHs.487540.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1OX-ray2.80A/D1-121[»]
1QUQX-ray2.50B/D1-121[»]
2PI2X-ray2.00E/F/G/H1-121[»]
2PQAX-ray2.50B/D1-121[»]
2Z6KX-ray3.00C/D1-121[»]
3KDFX-ray1.98A/C2-121[»]
ProteinModelPortalP35244.
SMRP35244. Positions 2-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112039. 43 interactions.
DIPDIP-24190N.
IntActP35244. 10 interactions.
MINTMINT-5002568.
STRING9606.ENSP00000223129.

PTM databases

PhosphoSiteP35244.

Polymorphism databases

DMDM464608.

Proteomic databases

PaxDbP35244.
PeptideAtlasP35244.
PRIDEP35244.

Protocols and materials databases

DNASU6119.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223129; ENSP00000223129; ENSG00000106399.
ENST00000396682; ENSP00000379914; ENSG00000106399.
GeneID6119.
KEGGhsa:6119.
UCSCuc003sri.3. human.

Organism-specific databases

CTD6119.
GeneCardsGC07M007643.
HGNCHGNC:10291. RPA3.
HPAHPA005708.
MIM179837. gene.
neXtProtNX_P35244.
PharmGKBPA34653.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42188.
HOGENOMHOG000252930.
HOVERGENHBG003004.
InParanoidP35244.
KOK10740.
OMAMELPKSR.
OrthoDBEOG77WWFG.
PhylomeDBP35244.
TreeFamTF105243.

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

ArrayExpressP35244.
BgeeP35244.
CleanExHS_RPA3.
GenevestigatorP35244.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR013970. Rep_factor-A_3.
[Graphical view]
PfamPF08661. Rep_fac-A_3. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRPA3. human.
EvolutionaryTraceP35244.
GeneWikiRPA3.
GenomeRNAi6119.
NextBio23763.
PROP35244.
SOURCESearch...

Entry information

Entry nameRFA3_HUMAN
AccessionPrimary (citable) accession number: P35244
Secondary accession number(s): Q549U6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 131 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 chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM