[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2050703 [NCBI, ExPASy, EBI, Israel, Japan]
Erdile L.F.,
Heyer W.-D.,
Kolodner R.,
Kelly T.J.;
"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.";
J. Biol. Chem. 266:12090-12098(1991).
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[2]
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SEQUENCE REVISION TO 217.
PubMed=8420996 [NCBI, ExPASy, EBI, Israel, Japan]
Erdile L.F.,
Heyer W.-D.,
Kolodner R.,
Kelly T.J.;
"Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing.";
J. Biol. Chem. 268:2268-2268(1993).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-351.
TISSUE=Aortic endothelium;
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.
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-351.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[6]
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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, AND MASS SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V.,
Vousden K.H.,
Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
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[7]
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INTERACTION WITH RPA4.
PubMed=7760808 [NCBI, ExPASy, EBI, Israel, Japan]
Keshav K.F.,
Chen C.,
Dutta A.;
"Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex.";
Mol. Cell. Biol. 15:3119-3128(1995).
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[8]
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INTERACTION WITH XPA.
DOI=10.1038/1400; PubMed=9699634 [NCBI, ExPASy, EBI, Israel, Japan]
Ikegami T.,
Kuraoka I.,
Saijo M.,
Kodo N.,
Kyogoku Y.,
Morikawa K.,
Tanaka K.,
Shirakawa M.;
"Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.";
Nat. Struct. Biol. 5:701-706(1998).
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[9]
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INTERACTION WITH XPA.
DOI=10.1021/bi991755p; PubMed=10563794 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.";
Biochemistry 38:15116-15128(1999).
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[10]
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INTERACTION WITH RIP.
DOI=10.1128/MCB.25.18.8202-8214.2005; PubMed=16135809 [NCBI, ExPASy, EBI, Israel, Japan]
Park J.,
Seo T.,
Kim H.,
Choe J.;
"Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies.";
Mol. Cell. Biol. 25:8202-8214(2005).
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[11]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
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[12]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N.,
Zhou C.,
Villen J.,
Beausoleil S.A.,
Bakalarski C.E.,
Elledge S.J.,
Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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[13]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[14]
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X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.
DOI=10.1038/385176a0; PubMed=8990123 [NCBI, ExPASy, EBI, Israel, Japan]
Bochkarev A.,
Pfuetzner R.A.,
Edwards A.M.,
Frappier L.;
"Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA.";
Nature 385:176-181(1997).
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