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P35244 (RFA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. 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.
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.7 Ref.8

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.7 Ref.8

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.7

Subcellular location

Nucleus.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121121Replication protein A 14 kDa subunit
PRO_0000097276

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]"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.
[8]"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.
[9]"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].
[10]"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.
IPIIPI00017373.
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.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-24190N.
IntActP35244. 9 interactions.
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.
OMATIMCASY.
OrthoDBEOG4NVZMT.
PhylomeDBP35244.

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.
GermOnlineENSG00000106399. Homo sapiens.

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. Nucleic_acid_OB. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRPA3. human.
EvolutionaryTraceP35244.
GenomeRNAi6119.
NextBio23763.
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: May 1, 2013
This is version 121 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

Human chromosome 7

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

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