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P27694 (RFA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 70 kDa DNA-binding subunit

Short name=RP-A p70
Alternative name(s):
Replication factor A protein 1
Short name=RF-A protein 1
Single-stranded DNA-binding protein
Gene names
Name:RPA1
Synonyms:REPA1, RPA70
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing. Ref.17 Ref.19

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.17 Ref.19

Subunit structure

Heterotrimer composed of RPA1, RPA2 and RPA3 (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 RPA1 subunit. Interacts with RIPK1 and XPA. Interacts with RPA4. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.20 Ref.23 Ref.25

Subcellular location

Nucleus.

Post-translational modification

Sumoylated on lysine residues Lys-449 and Lys-577, with Lys-449 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6. Ref.20

Sequence similarities

Belongs to the replication factor A protein 1 family.

Contains 1 OB DNA-binding domain.

Sequence caution

The sequence BAD92969.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombinase assembly

Traceable author statement. Source: Reactome

DNA recombination

Traceable author statement PubMed 8756712. Source: ProtInc

DNA repair

Traceable author statement. Source: Reactome

DNA replication

Inferred from mutant phenotype PubMed 9430682. Source: UniProtKB

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

DNA-dependent DNA replication

Traceable author statement PubMed 8756712. Source: ProtInc

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

base-excision repair

Inferred from direct assay PubMed 9765279. Source: UniProtKB

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

meiotic nuclear division

Inferred from electronic annotation. Source: Ensembl

mismatch repair

Inferred from mutant phenotype PubMed 9430682. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Inferred from mutant phenotype PubMed 9430682. Source: UniProtKB

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Traceable author statement. Source: Reactome

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from physical interaction. Source: MGI

PML body

Inferred from direct assay Ref.13. Source: MGI

actin cytoskeleton

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

lateral element

Inferred from electronic annotation. Source: Ensembl

male germ cell nucleus

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Inferred from direct assay PubMed 7700386. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10825162PubMed 1311258PubMed 15897895PubMed 7700386. Source: UniProtKB

single-stranded DNA binding

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 616616Replication protein A 70 kDa DNA-binding subunit
PRO_0000423231
Initiator methionine11Removed; alternate Ref.8
Chain2 – 616615Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
PRO_0000097260

Regions

DNA binding197 – 28185OB
Zinc finger481 – 50323C4-type Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16 Ref.24
Modified residue1631N6-acetyllysine Ref.18
Modified residue1671N6-acetyllysine Ref.18
Modified residue1801Phosphothreonine Ref.14 Ref.21
Modified residue1911Phosphothreonine Ref.21
Modified residue2591N6-acetyllysine Ref.18
Modified residue3841Phosphoserine Ref.21
Cross-link449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20
Cross-link577Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20

Natural variations

Natural variant3511T → A. Ref.4 Ref.5
Corresponds to variant rs5030755 [ dbSNP | Ensembl ].
VAR_019236

Experimental info

Mutagenesis411R → E: Loss of HELB-binding; when associated with E-43. Ref.23
Mutagenesis431R → E: Loss of HELB-binding; when associated with E-41. Ref.23
Mutagenesis4491K → R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577. Ref.20
Mutagenesis5771K → R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449. Ref.20

Secondary structure

.................................................................................................... 616
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27694 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: FE038F40F5886CD1

FASTA61668,138
        10         20         30         40         50         60 
MVGQLSEGAI AAIMQKGDTN IKPILQVINI RPITTGNSPP RYRLLMSDGL NTLSSFMLAT 

        70         80         90        100        110        120 
QLNPLVEEEQ LSSNCVCQIH RFIVNTLKDG RRVVILMELE VLKSAEAVGV KIGNPVPYNE 

       130        140        150        160        170        180 
GLGQPQVAPP APAASPAASS RPQPQNGSSG MGSTVSKAYG ASKTFGKAAG PSLSHTSGGT 

       190        200        210        220        230        240 
QSKVVPIASL TPYQSKWTIC ARVTNKSQIR TWSNSRGEGK LFSLELVDES GEIRATAFNE 

       250        260        270        280        290        300 
QVDKFFPLIE VNKVYYFSKG TLKIANKQFT AVKNDYEMTF NNETSVMPCE DDHHLPTVQF 

       310        320        330        340        350        360 
DFTGIDDLEN KSKDSLVDII GICKSYEDAT KITVRSNNRE VAKRNIYLMD TSGKVVTATL 

       370        380        390        400        410        420 
WGEDADKFDG SRQPVLAIKG ARVSDFGGRS LSVLSSSTII ANPDIPEAYK LRGWFDAEGQ 

       430        440        450        460        470        480 
ALDGVSISDL KSGGVGGSNT NWKTLYEVKS ENLGQGDKPD YFSSVATVVY LRKENCMYQA 

       490        500        510        520        530        540 
CPTQDCNKKV IDQQNGLYRC EKCDTEFPNF KYRMILSVNI ADFQENQWVT CFQESAEAIL 

       550        560        570        580        590        600 
GQNAAYLGEL KDKNEQAFEE VFQNANFRSF IFRVRVKVET YNDESRIKAT VMDVKPVDYR 

       610 
EYGRRLVMSI RRSALM 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding subunit of human replication protein A and the role of the protein in DNA replication."
Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.
J. Biol. Chem. 266:12090-12098(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing."
Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.
J. Biol. Chem. 268:2268-2268(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 217.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-351.
Tissue: Aortic endothelium.
[5]NIEHS SNPs program
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-351.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Uterus.
[8]Bienvenut W.V., Vousden K.H., Lukashchuk N.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-41; 82-88; 93-103; 168-196; 221-259; 314-324; 345-379; 390-410; 413-472; 490-499; 503-511; 552-568; 576-586 AND 589-600, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[9]"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.
[10]"Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms."
Braun K.A., Lao Y., He Z., Ingles C.J., Wold M.S.
Biochemistry 36:8443-8454(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POLA1.
[11]"Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA."
Ikegami T., Kuraoka I., Saijo M., Kodo N., Kyogoku Y., Morikawa K., Tanaka K., Shirakawa M.
Nat. Struct. Biol. 5:701-706(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPA.
[12]"Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies."
Buchko G.W., Daughdrill G.W., de Lorimier R., Sudha Rao B.K., Isern N.G., Lingbeck J.M., Taylor J.-S., Wold M.S., Gochin M., Spicer L.D., Lowry D.F., Kennedy M.A.
Biochemistry 38:15116-15128(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPA.
[13]"Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies."
Park J., Seo T., Kim H., Choe J.
Mol. Cell. Biol. 25:8202-8214(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIPK1.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-167 AND LYS-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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.
[20]"Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex."
Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.
Mol. Cell 39:333-345(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-449 AND LYS-577, DESUMOYLATION BY SENP6, MUTAGENESIS OF LYS-449 AND LYS-577, INTERACTION WITH SENP6 AND RAD51.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180; THR-191 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress."
Guler G.D., Liu H., Vaithiyalingam S., Arnett D.R., Kremmer E., Chazin W.J., Fanning E.
J. Biol. Chem. 287:6469-6481(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HELB, MUTAGENESIS OF ARG-41 AND ARG-43.
[24]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity."
Wan L., Lou J., Xia Y., Su B., Liu T., Cui J., Sun Y., Lou H., Huang J.
EMBO Rep. 14:1104-1112(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRIMPOL.
[26]"Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA."
Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L.
Nature 385:176-181(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63488 mRNA. Translation: AAA36584.1.
AK289704 mRNA. Translation: BAF82393.1.
AB209732 mRNA. Translation: BAD92969.1. Different initiation.
AY599563 Genomic DNA. Translation: AAS94324.1.
CH471108 Genomic DNA. Translation: EAW90574.1.
BC018126 mRNA. Translation: AAH18126.1.
CCDSCCDS11014.1.
PIRA40457.
RefSeqNP_002936.1. NM_002945.3.
UniGeneHs.461925.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EWINMR-A1-114[»]
1FGUX-ray2.50A/B182-432[»]
1JMCX-ray2.40A181-422[»]
1L1OX-ray2.80C/F436-616[»]
2B29X-ray1.60A1-120[»]
2B3GX-ray1.60A1-120[»]
4IJHX-ray1.50A1-120[»]
4IJLX-ray1.70A1-120[»]
4IPCX-ray1.22A1-120[»]
4IPDX-ray1.51A1-120[»]
4IPGX-ray1.58A1-120[»]
4IPHX-ray1.94A1-120[»]
4LUOX-ray1.54A1-120[»]
4LUVX-ray1.40A1-120[»]
4LUZX-ray1.90A1-120[»]
4LW1X-ray1.63A1-120[»]
4LWCX-ray1.61A1-120[»]
4NB3X-ray1.35A/B1-120[»]
4O0AX-ray1.20A1-120[»]
DisProtDP00061.
ProteinModelPortalP27694.
SMRP27694. Positions 3-120, 183-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112037. 445 interactions.
DIPDIP-24189N.
IntActP27694. 42 interactions.
MINTMINT-91488.
STRING9606.ENSP00000254719.

Chemistry

BindingDBP27694.
ChEMBLCHEMBL1764940.

PTM databases

PhosphoSiteP27694.

Polymorphism databases

DMDM1350579.

Proteomic databases

MaxQBP27694.
PaxDbP27694.
PeptideAtlasP27694.
PRIDEP27694.

Protocols and materials databases

DNASU6117.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254719; ENSP00000254719; ENSG00000132383.
GeneID6117.
KEGGhsa:6117.
UCSCuc002fto.2. human.

Organism-specific databases

CTD6117.
GeneCardsGC17P001680.
HGNCHGNC:10289. RPA1.
HPACAB004563.
HPA006914.
HPA046497.
MIM179835. gene.
neXtProtNX_P27694.
PharmGKBPA34651.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1599.
HOGENOMHOG000162322.
HOVERGENHBG010502.
InParanoidP27694.
KOK07466.
OMAYQACPSQ.
OrthoDBEOG7GXPBM.
PhylomeDBP27694.
TreeFamTF105241.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP27694.
BgeeP27694.
CleanExHS_RPA1.
GenevestigatorP27694.

Family and domain databases

Gene3D2.40.50.140. 4 hits.
InterProIPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
IPR013955. Rep_factor-A_C.
IPR007199. Rep_factor-A_N.
IPR004591. Rep_factor_Rpa1.
[Graphical view]
PfamPF04057. Rep-A_N. 1 hit.
PF08646. Rep_fac-A_C. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 4 hits.
TIGRFAMsTIGR00617. rpa1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRPA1. human.
EvolutionaryTraceP27694.
GeneWikiReplication_protein_A1.
GenomeRNAi6117.
NextBio23755.
PROP27694.
SOURCESearch...

Entry information

Entry nameRFA1_HUMAN
AccessionPrimary (citable) accession number: P27694
Secondary accession number(s): A8K0Y9, Q59ES9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 155 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

SIMILARITY comments

Index of protein domains and families

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM