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Protein

Replication protein A 30 kDa subunit

Gene

RPA4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support 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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi74 – 14875OBAdd
BLAST

GO - Molecular functioni

  • single-stranded DNA binding Source: ProtInc

GO - Biological processi

  • DNA damage checkpoint Source: UniProtKB
  • DNA recombination Source: InterPro
  • DNA replication initiation Source: ProtInc
  • G1/S transition of mitotic cell cycle Source: Reactome
  • mitotic cell cycle Source: Reactome
  • nucleotide-excision repair Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-68962. Activation of the pre-replicative complex.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RPA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:30305. RPA4.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Localizes to DNA repair foci after DNA damage.

GO - Cellular componenti

  • DNA replication factor A complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134988548.

Polymorphism and mutation databases

BioMutaiRPA4.
DMDMi14917036.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Replication protein A 30 kDa subunitPRO_0000097280Add
BLAST

Proteomic databases

PaxDbiQ13156.
PRIDEiQ13156.

PTM databases

PhosphoSiteiQ13156.

Expressioni

Tissue specificityi

Preferentially expressed in placental and colon mucosa. Widely expressed at intermediate or lower levels.1 Publication

Gene expression databases

BgeeiQ13156.
CleanExiHS_RPA4.
GenevisibleiQ13156. HS.

Interactioni

Subunit structurei

Component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2. Interacts with RPA1 and RPA3.2 Publications

Protein-protein interaction databases

BioGridi118975. 13 interactions.
DIPiDIP-24241N.
IntActiQ13156. 1 interaction.
STRINGi9606.ENSP00000362131.

Structurei

3D structure databases

ProteinModelPortaliQ13156.
SMRiQ13156. Positions 46-170, 202-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000010045.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiQ13156.
KOiK10741.
OMAiAHMMLDK.
OrthoDBiEOG76X615.
PhylomeDBiQ13156.
TreeFamiTF105242.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR014646. Rfa2/RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08784. RPA_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036949. RPA32. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Q13156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSGFGSYG SISAADGASG GSDQLCERDA TPAIKTQRPK VRIQDVVPCN
60 70 80 90 100
VNQLLSSTVF DPVFKVRGII VSQVSIVGVI RGAEKASNHI CYKIDDMTAK
110 120 130 140 150
PIEARQWFGR EKVKQVTPLS VGVYVKVFGI LKCPTGTKSL EVLKIHVLED
160 170 180 190 200
MNEFTVHILE TVNAHMMLDK ARRDTTVESV PVSPSEVNDA GDNDESHRNF
210 220 230 240 250
IQDEVLRLIH ECPHQEGKSI HELRAQLCDL SVKAIKEAID YLTVEGHIYP
260
TVDREHFKSA D
Length:261
Mass (Da):28,868
Last modified:July 11, 2001 - v2
Checksum:i6A925FAEDBE21718
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331A → T.1 Publication
Corresponds to variant rs2642219 [ dbSNP | Ensembl ].
VAR_019170

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35345.1.
RefSeqiNP_037479.1. NM_013347.4.
UniGeneiHs.659349.

Genome annotation databases

EnsembliENST00000373040; ENSP00000362131; ENSG00000204086.
GeneIDi29935.
KEGGihsa:29935.
UCSCiuc004efv.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35345.1.
RefSeqiNP_037479.1. NM_013347.4.
UniGeneiHs.659349.

3D structure databases

ProteinModelPortaliQ13156.
SMRiQ13156. Positions 46-170, 202-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118975. 13 interactions.
DIPiDIP-24241N.
IntActiQ13156. 1 interaction.
STRINGi9606.ENSP00000362131.

PTM databases

PhosphoSiteiQ13156.

Polymorphism and mutation databases

BioMutaiRPA4.
DMDMi14917036.

Proteomic databases

PaxDbiQ13156.
PRIDEiQ13156.

Protocols and materials databases

DNASUi29935.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373040; ENSP00000362131; ENSG00000204086.
GeneIDi29935.
KEGGihsa:29935.
UCSCiuc004efv.5. human.

Organism-specific databases

CTDi29935.
GeneCardsiRPA4.
HGNCiHGNC:30305. RPA4.
MIMi300767. gene.
neXtProtiNX_Q13156.
PharmGKBiPA134988548.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000010045.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiQ13156.
KOiK10741.
OMAiAHMMLDK.
OrthoDBiEOG76X615.
PhylomeDBiQ13156.
TreeFamiTF105242.

Enzyme and pathway databases

ReactomeiR-HSA-68962. Activation of the pre-replicative complex.

Miscellaneous databases

GeneWikiiRPA4.
GenomeRNAii29935.
NextBioi52579.
PROiQ13156.
SOURCEiSearch...

Gene expression databases

BgeeiQ13156.
CleanExiHS_RPA4.
GenevisibleiQ13156. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR014646. Rfa2/RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08784. RPA_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036949. RPA32. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRFA4_HUMAN
AccessioniPrimary (citable) accession number: Q13156
Secondary accession number(s): Q3SY03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2001
Last modified: March 16, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.