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Replication protein A 14 kDa subunit (RP-A p14) (Replication factor A protein 3) (RF-A protein 3)

 RFA3_HUMAN              Reviewed;         121 AA.
P35244; Q549U6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 166.
RecName: Full=Replication protein A 14 kDa subunit;
Short=RP-A p14;
AltName: Full=Replication factor A protein 3;
Short=RF-A protein 3;
Name=RPA3; Synonyms=REPA3, RPA14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8454588;
Umbricht C.B., Kelly T.J.;
"Cloning, overexpression, and genomic mapping of the 14-kDa subunit of
human replication protein A.";
J. Biol. Chem. 268:6131-6138(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
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., 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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
PubMed=7697716; DOI=10.1016/0092-8674(95)90289-9;
Aboussekhra A., Biggerstaff M., Shivji M.K., Vilpo J.A., Moncollin V.,
Podust V.N., Protic M., Huebscher U., Egly J.M., Wood R.D.;
"Mammalian DNA nucleotide excision repair reconstituted with purified
protein components.";
Cell 80:859-868(1995).
[7]
INTERACTION WITH RPA4.
PubMed=7760808; DOI=10.1128/MCB.15.6.3119;
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).
[8]
FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, AND
FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
PubMed=9430682; DOI=10.1074/jbc.273.3.1453;
Lin Y.L., Shivji M.K., Chen C., Kolodner R., Wood R.D., Dutta A.;
"The evolutionarily conserved zinc finger motif in the largest subunit
of human replication protein A is required for DNA replication and
mismatch repair but not for nucleotide excision repair.";
J. Biol. Chem. 273:1453-1461(1998).
[9]
FUNCTION IN BASE EXCISION REPAIR.
PubMed=9765279; DOI=10.1074/jbc.273.42.27492;
DeMott M.S., Zigman S., Bambara R.A.;
"Replication protein A stimulates long patch DNA base excision
repair.";
J. Biol. Chem. 273:27492-27498(1998).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION IN THE ARPA COMPLEX, AND FUNCTION OF THE ARPA COMPLEX.
PubMed=19116208; DOI=10.1074/jbc.M808963200;
Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F.,
Wold M.S.;
"An alternative form of replication protein a prevents viral
replication in vitro.";
J. Biol. Chem. 284:5324-5331(2009).
[12]
SINGLE-STRANDED DNA-BINDING.
PubMed=19010961; DOI=10.1093/nar/gkn895;
Salas T.R., Petruseva I., Lavrik O., Saintome C.;
"Evidence for direct contact between the RPA3 subunit of the human
replication protein A and single-stranded DNA.";
Nucleic Acids Res. 37:38-46(2009).
[13]
FUNCTION OF THE ARPA COMPLEX.
PubMed=19996105; DOI=10.1074/jbc.M109.079418;
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.;
"An alternative form of replication protein a expressed in normal
human tissues supports DNA repair.";
J. Biol. Chem. 285:4788-4797(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
FUNCTION.
PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002;
Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D.,
Liu S., Jimenez A.E., Jin J., Zou L.;
"PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and
drives ATR activation via a ubiquitin-mediated circuitry.";
Mol. Cell 53:235-246(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
UBIQUITINATION AT LYS-23; LYS-39 AND LYS-88.
PubMed=26474068; DOI=10.1016/j.molcel.2015.09.011;
Elia A.E., Wang D.C., Willis N.A., Boardman A.P., Hajdu I.,
Adeyemi R.O., Lowry E., Gygi S.P., Scully R., Elledge S.J.;
"RFWD3-dependent ubiquitination of RPA regulates repair at stalled
replication forks.";
Mol. Cell 60:280-293(2015).
[21]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RPA1 AND RPA2.
PubMed=11927569; DOI=10.1093/emboj/21.7.1855;
Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.;
"Structure of the RPA trimerization core and its role in the multistep
DNA-binding mechanism of RPA.";
EMBO J. 21:1855-1863(2002).
-!- FUNCTION: As part of the heterotrimeric replication protein A
complex (RPA/RP-A), binds and stabilizes single-stranded DNA
intermediates that form during DNA replication or upon DNA stress.
It prevents their reannealing and in parallel, recruits and
activates different proteins and complexes involved in DNA
metabolism. Thereby, it plays an essential role both in DNA
replication and the cellular response to DNA damage
(PubMed:9430682). In the cellular response to DNA damage, the RPA
complex controls DNA repair and DNA damage checkpoint activation.
Through recruitment of ATRIP activates the ATR kinase a master
regulator of the DNA damage response (PubMed:24332808). It is
required for the recruitment of the DNA double-strand break repair
factors RAD51 and RAD52 to chromatin, in response to DNA damage.
Also recruits to sites of DNA damage proteins like XPA and XPG
that are involved in nucleotide excision repair and is required
for this mechanism of DNA repair (PubMed:7697716). Plays also a
role in base excision repair (BER), probably through interaction
with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is
involved in replication fork restart, to sites of DNA damage. May
also play a role in telomere maintenance. RPA3 has its own single-
stranded DNA-binding activity and may be responsible for polarity
of the binding of the complex to DNA (PubMed:19010961). 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 synthesis by polymerase
delta in presence of PCNA and replication factor C (RFC), the dual
incision/excision reaction of nucleotide excision repair and
RAD51-dependent strand exchange (PubMed:19996105).
{ECO:0000269|PubMed:19010961, ECO:0000269|PubMed:19116208,
ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:7697716,
ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279,
ECO:0000303|PubMed:24332808}.
-!- SUBUNIT: Component of the canonical replication protein A complex
(RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also
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. {ECO:0000269|PubMed:11927569,
ECO:0000269|PubMed:19116208}.
-!- INTERACTION:
P43351:RAD52; NbExp=3; IntAct=EBI-621428, EBI-706448;
P27694:RPA1; NbExp=8; IntAct=EBI-621428, EBI-621389;
P15927:RPA2; NbExp=8; IntAct=EBI-621428, EBI-621404;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Ubiquitinated by RFWD3 at stalled replication forks in
response to DNA damage: ubiquitination by RFWD3 does not lead to
degradation by the proteasome and promotes removal of the RPA
complex from stalled replication forks, promoting homologous
recombination (PubMed:26474068). {ECO:0000269|PubMed:26474068}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rpa3/";
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EMBL; L07493; AAA58350.1; -; mRNA.
EMBL; BT007320; AAP35984.1; -; mRNA.
EMBL; DQ003136; AAX84517.1; -; Genomic_DNA.
EMBL; AC004948; AAQ96878.1; -; Genomic_DNA.
EMBL; BC005264; AAH05264.1; -; mRNA.
EMBL; BC009868; AAH09868.1; -; mRNA.
CCDS; CCDS5356.1; -.
PIR; A46008; A46008.
RefSeq; NP_002938.1; NM_002947.4.
UniGene; Hs.487540; -.
PDB; 1L1O; X-ray; 2.80 A; A/D=1-121.
PDB; 1QUQ; X-ray; 2.50 A; B/D=1-121.
PDB; 2PI2; X-ray; 2.00 A; E/F/G/H=1-121.
PDB; 2PQA; X-ray; 2.50 A; B/D=1-121.
PDB; 2Z6K; X-ray; 3.00 A; C/D=1-121.
PDB; 3KDF; X-ray; 1.98 A; A/C=1-121.
PDBsum; 1L1O; -.
PDBsum; 1QUQ; -.
PDBsum; 2PI2; -.
PDBsum; 2PQA; -.
PDBsum; 2Z6K; -.
PDBsum; 3KDF; -.
ProteinModelPortal; P35244; -.
SMR; P35244; -.
BioGrid; 112039; 390.
CORUM; P35244; -.
DIP; DIP-24190N; -.
IntAct; P35244; 28.
MINT; MINT-5002568; -.
STRING; 9606.ENSP00000223129; -.
iPTMnet; P35244; -.
PhosphoSitePlus; P35244; -.
BioMuta; RPA3; -.
DMDM; 464608; -.
EPD; P35244; -.
MaxQB; P35244; -.
PaxDb; P35244; -.
PeptideAtlas; P35244; -.
PRIDE; P35244; -.
TopDownProteomics; P35244; -.
DNASU; 6119; -.
Ensembl; ENST00000223129; ENSP00000223129; ENSG00000106399.
Ensembl; ENST00000396682; ENSP00000379914; ENSG00000106399.
GeneID; 6119; -.
KEGG; hsa:6119; -.
UCSC; uc003sri.4; human.
CTD; 6119; -.
DisGeNET; 6119; -.
EuPathDB; HostDB:ENSG00000106399.11; -.
GeneCards; RPA3; -.
HGNC; HGNC:10291; RPA3.
HPA; HPA005708; -.
MIM; 179837; gene.
neXtProt; NX_P35244; -.
OpenTargets; ENSG00000106399; -.
PharmGKB; PA34653; -.
eggNOG; ENOG410IZRM; Eukaryota.
eggNOG; ENOG4111REI; LUCA.
GeneTree; ENSGT00390000008029; -.
HOGENOM; HOG000252930; -.
HOVERGEN; HBG003004; -.
InParanoid; P35244; -.
KO; K10740; -.
OMA; KPRINCS; -.
OrthoDB; EOG091G1178; -.
PhylomeDB; P35244; -.
TreeFam; TF105243; -.
Reactome; R-HSA-110312; Translesion synthesis by REV1.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-5655862; Translesion synthesis by POLK.
Reactome; R-HSA-5656121; Translesion synthesis by POLI.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-68962; Activation of the pre-replicative complex.
Reactome; R-HSA-69166; Removal of the Flap Intermediate.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-912446; Meiotic recombination.
ChiTaRS; RPA3; human.
EvolutionaryTrace; P35244; -.
GeneWiki; RPA3; -.
GenomeRNAi; 6119; -.
PRO; PR:P35244; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106399; -.
CleanEx; HS_RPA3; -.
ExpressionAtlas; P35244; baseline and differential.
Genevisible; P35244; HS.
GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0006298; P:mismatch repair; IMP:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0000723; P:telomere maintenance; TAS:BHF-UCL.
GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR013970; Rfa2.
Pfam; PF08661; Rep_fac-A_3; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; DNA damage;
DNA recombination; DNA repair; DNA replication; Isopeptide bond;
Nucleus; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 121 Replication protein A 14 kDa subunit.
/FTId=PRO_0000097276.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:26474068}.
CROSSLNK 39 39 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:26474068}.
CROSSLNK 88 88 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:26474068}.
HELIX 4 6 {ECO:0000244|PDB:3KDF}.
STRAND 10 12 {ECO:0000244|PDB:3KDF}.
HELIX 14 20 {ECO:0000244|PDB:3KDF}.
STRAND 24 34 {ECO:0000244|PDB:3KDF}.
STRAND 38 44 {ECO:0000244|PDB:3KDF}.
STRAND 50 54 {ECO:0000244|PDB:3KDF}.
STRAND 65 73 {ECO:0000244|PDB:3KDF}.
STRAND 79 86 {ECO:0000244|PDB:3KDF}.
STRAND 90 92 {ECO:0000244|PDB:3KDF}.
HELIX 96 108 {ECO:0000244|PDB:3KDF}.
HELIX 110 112 {ECO:0000244|PDB:3KDF}.
SEQUENCE 121 AA; 13569 MW; 3FD99851959FB498 CRC64;
MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN GTIELMEPLD
EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN EAVKIIHDFP QFYPLGIVQH
D


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EIAAB34345 Homo sapiens,Human,REPA2,Replication factor A protein 2,Replication protein A 32 kDa subunit,Replication protein A 34 kDa subunit,RF-A protein 2,RP-A p32,RP-A p34,RPA2,RPA32,RPA34
EIAAB34346 Mouse,Mus musculus,Replication factor A protein 2,Replication protein A 32 kDa subunit,Replication protein A 34 kDa subunit,RF-A protein 2,RP-A p32,RP-A p34,Rpa2,Rpa34
EIAAB34348 Homo sapiens,Human,REPA3,Replication factor A protein 3,Replication protein A 14 kDa subunit,RF-A protein 3,RP-A p14,RPA14,RPA3
EIAAB34350 Homo sapiens,Human,Replication factor A protein 4,Replication protein A 30 kDa subunit,RF-A protein 4,RP-A p30,RPA4
EIAAB34343 Mouse,Mus musculus,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,Rpa1
EIAAB34349 Mouse,Mus musculus,Replication factor A protein 3,Replication protein A 14 kDa subunit,RF-A protein 3,RP-A p14,Rpa3
EIAAB34347 Rat,Rattus norvegicus,Replication factor A protein 2,Replication protein A 32 kDa subunit,RF-A protein 2,RP-A p32,Rpa2
EIAAB34342 Homo sapiens,Human,REPA1,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,RPA1,RPA70,Single-stranded DNA-binding protein
EIAAB34344 Chicken,Gallus gallus,RCJMB04_17l6,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,RPA1
15-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 Polyclonal 0.1 mg
15-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 Polyclonal 0.05 mg
10-288-22181F Replication protein A 32 kDa subunit - RP-A; RF-A; Replication factor-A protein 2; p32; p34 0.05 mg
10-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 0.05 mg
10-288-22181F Replication protein A 32 kDa subunit - RP-A; RF-A; Replication factor-A protein 2; p32; p34 0.1 mg
10-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 0.1 mg
EIAAB34352 A1 140 kDa subunit,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,DNA-binding protein PO-GA,Homo sapiens,Human,Replication factor C 140 kDa subunit,Replication factor C la
20-372-60021 replication protein A1. 70kDa (RPA1) - Mouse monoclonal anti-human RPA1 antibody; RP-A; RF-A; Replication factor-A protein 1; Single-stranded DNA-binding protein; p70 Monoclonal 0.1 mg
20-372-60276 replication protein A2. 32kDa (RPA2) - Mouse monoclonal anti-human RPA2 antibody; RP-A; RF-A; Replication factor-A protein 2; p32; p34 Monoclonal 0.1 mg
EIAAB34355 A1 40 kDa subunit,Activator 1 40 kDa subunit,Activator 1 subunit 2,Homo sapiens,Human,Replication factor C 40 kDa subunit,Replication factor C subunit 2,RF-C 40 kDa subunit,RFC2,RFC40
EIAAB34360 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Homo sapiens,Human,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,RFC3,RFC38
EIAAB34361 A1 37 kDa subunit,Activator 1 37 kDa subunit,Activator 1 subunit 4,Homo sapiens,Human,Replication factor C 37 kDa subunit,Replication factor C subunit 4,RF-C 37 kDa subunit,RFC37,RFC4
EIAAB34363 A1 36 kDa subunit,Activator 1 36 kDa subunit,Activator 1 subunit 5,Homo sapiens,Human,Replication factor C 36 kDa subunit,Replication factor C subunit 5,RF-C 36 kDa subunit,RFC36,RFC5
EIAAB34273 60 kDa origin-specific DNA-binding protein,60 kDa replication initiation region protein,ATT-binding protein,DHFR oribeta-binding protein RIP60,Homo sapiens,Human,REPIN1,Replication initiator 1,RIP60,Z
5008 Protein,Replication factor C subunit 3 0.1 mg
5144 Protein,Replication factor C subunit 5 0.1 mg


 

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