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Q13156 (RFA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Replication protein A 30 kDa subunit

Short name=RP-A p30
Alternative name(s):
Replication factor A protein 4
Short name=RF-A protein 4
Gene names
Name:RPA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.6 Ref.7 Ref.8 Ref.9

Subunit structure

Component of the alternative replication protein A complex (aRPA) composed of RPA1, RPA3 and RPA4. Interacts with RPA1 and RPA3. Ref.1 Ref.6

Subcellular location

Nucleus. Note: Localizes to DNA repair foci after DNA damage. Ref.9

Tissue specificity

Preferentially expressed in placental and colon mucosa. Widely expressed at intermediate or lower levels. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Replication protein A 30 kDa subunit
PRO_0000097280

Natural variations

Natural variant331A → T. Ref.3
Corresponds to variant rs2642219 [ dbSNP | Ensembl ].
VAR_019170

Sequences

Sequence LengthMass (Da)Tools
Q13156 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 6A925FAEDBE21718

FASTA26128,868
        10         20         30         40         50         60 
MSKSGFGSYG SISAADGASG GSDQLCERDA TPAIKTQRPK VRIQDVVPCN VNQLLSSTVF 

        70         80         90        100        110        120 
DPVFKVRGII VSQVSIVGVI RGAEKASNHI CYKIDDMTAK PIEARQWFGR EKVKQVTPLS 

       130        140        150        160        170        180 
VGVYVKVFGI LKCPTGTKSL EVLKIHVLED MNEFTVHILE TVNAHMMLDK ARRDTTVESV 

       190        200        210        220        230        240 
PVSPSEVNDA GDNDESHRNF IQDEVLRLIH ECPHQEGKSI HELRAQLCDL SVKAIKEAID 

       250        260 
YLTVEGHIYP TVDREHFKSA D 

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References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH RPA1 AND RPA3.
[2]Keshav K.F.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 10.
[3]NIEHS SNPs program
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-33.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [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].
[6]"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.
[7]"Functions of alternative replication protein A in initiation and elongation."
Mason A.C., Roy R., Simmons D.T., Wold M.S.
Biochemistry 49:5919-5928(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, TISSUE SPECIFICITY.
[9]"A naturally occurring human RPA subunit homolog does not support DNA replication or cell-cycle progression."
Haring S.J., Humphreys T.D., Wold M.S.
Nucleic Acids Res. 38:846-858(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24186 mRNA. Translation: AAB08488.2.
AF494047 Genomic DNA. Translation: AAM09569.1.
Z86061 Genomic DNA. Translation: CAI42256.1.
BC069791 mRNA. Translation: AAH69791.1.
BC069808 mRNA. Translation: AAH69808.1.
BC069824 mRNA. Translation: AAH69824.1.
BC104013 mRNA. Translation: AAI04014.1.
BC104014 mRNA. Translation: AAI04015.1.
IPIIPI00011917.
RefSeqNP_037479.1. NM_013347.4.
UniGeneHs.659349.

3D structure databases

ProteinModelPortalQ13156.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-24241N.
IntActQ13156. 1 interaction.
STRING9606.ENSP00000362131.

PTM databases

PhosphoSiteQ13156.

Polymorphism databases

DMDM14917036.

Proteomic databases

PaxDbQ13156.
PRIDEQ13156.

Protocols and materials databases

DNASU29935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373040; ENSP00000362131; ENSG00000204086.
GeneID29935.
KEGGhsa:29935.
UCSCuc004efv.4. human.

Organism-specific databases

CTD29935.
GeneCardsGC0XP096139.
HGNCHGNC:30305. RPA4.
MIM300767. gene.
neXtProtNX_Q13156.
PharmGKBPA134988548.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325006.
HOGENOMHOG000216562.
HOVERGENHBG000086.
InParanoidQ13156.
KOK10741.
OMAVGVYAKV.
OrthoDBEOG4WQ13T.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

BgeeQ13156.
CleanExHS_RPA4.
GenevestigatorQ13156.
GermOnlineENSG00000204086. Homo sapiens.

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-helicase.
IPR014646. RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF08784. RPA_C. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PIRSFPIRSF036949. RPA32. 1 hit.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi29935.
NextBio52579.
SOURCESearch...

Entry information

Entry nameRFA4_HUMAN
AccessionPrimary (citable) accession number: Q13156
Secondary accession number(s): Q3SY03
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2001
Last modified: May 1, 2013
This is version 100 of the entry and version 2 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 X

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

Human entries with polymorphisms or disease mutations

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