P35244 (RFA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Replication protein A 14 kDa subunit
Short name=RP-A p14

Alternative name(s):
Replication factor A protein 3
Short name=RF-A protein 3

Gene names

Name:	RPA3
Synonyms:	REPA3, RPA14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Ref.7 Ref.8 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.7 Ref.8
Subunit structure	Heterotrimer of 70, 32 and 14 kDa chains (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 70 kDa subunit. Interacts with RPA4. Ref.6 Ref.7
Subcellular location	Nucleus.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombinase assembly Traceable author statement. Source: Reactome DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome nucleotide-excision repair, DNA gap filling 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_component	DNA replication factor A complex Traceable author statement Ref.1. Source: ProtInc cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	single-stranded DNA binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAD52	P43351	2	EBI-621428,EBI-706448
RPA1	P27694	4	EBI-621428,EBI-621389
RPA2	P15927	3	EBI-621428,EBI-621404

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 121

121

Replication protein A 14 kDa subunit

PRO_0000097276

Secondary structure

1

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121

Helix Strand Turn

Details...

Helix

4 – 6

3

Beta strand

10 – 12

3

Helix

14 – 20

7

Beta strand

24 – 34

11

Beta strand

38 – 44

7

Beta strand

50 – 54

5

Beta strand

65 – 73

9

Beta strand

79 – 86

8

Beta strand

90 – 92

3

Helix

96 – 108

13

Helix

110 – 112

3

Sequences

	Sequence		Length	Mass (Da)
	P35244 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 3FD99851959FB498	FASTA	121	13,569
	10 20 30 40 50 60 MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN GTIELMEPLD 70 80 90 100 110 120 EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN EAVKIIHDFP QFYPLGIVQH D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A." Umbricht C.B., Kelly T.J. J. Biol. Chem. 268:6131-6138(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIEHS SNPs program Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence of human chromosome 7." 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. Nature 424:157-164(2003) [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]. Tissue: Kidney and Lung.
[6]	"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.
[7]	"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.
[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.
[9]	"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].
[10]	"Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA." Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A. EMBO J. 21:1855-1863(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RPA1 AND RPA2.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07493 mRNA. Translation: AAA58350.1.
BT007320 mRNA. Translation: AAP35984.1.
DQ003136 Genomic DNA. Translation: AAX84517.1.
AC004948 Genomic DNA. Translation: AAQ96878.1.
BC005264 mRNA. Translation: AAH05264.1.
BC009868 mRNA. Translation: AAH09868.1.

IPI

IPI00017373.

PIR

A46008.

RefSeq

NP_002938.1. NM_002947.3.

UniGene

Hs.487540.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L1O	X-ray	2.80	A/D	1-121	[»]
1QUQ	X-ray	2.50	B/D	1-121	[»]
2PI2	X-ray	2.00	E/F/G/H	1-121	[»]
2PQA	X-ray	2.50	B/D	1-121	[»]
2Z6K	X-ray	3.00	C/D	1-121	[»]
3KDF	X-ray	1.98	A/C	2-121	[»]

ProteinModelPortal

P35244.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24190N.

IntAct

P35244. 9 interactions.

STRING

9606.ENSP00000223129.

PTM databases

PhosphoSite

P35244.

Polymorphism databases

DMDM

464608.

Proteomic databases

PaxDb

P35244.

PeptideAtlas

P35244.

PRIDE

P35244.

Protocols and materials databases

DNASU

6119.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000223129; ENSP00000223129; ENSG00000106399.
ENST00000396682; ENSP00000379914; ENSG00000106399.

GeneID

6119.

KEGG

hsa:6119.

UCSC

uc003sri.3. human.

Organism-specific databases

CTD

6119.

GeneCards

GC07M007643.

HGNC

HGNC:10291. RPA3.

HPA

HPA005708.

MIM

179837. gene.

neXtProt

NX_P35244.

PharmGKB

PA34653.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42188.

HOGENOM

HOG000252930.

HOVERGEN

HBG003004.

InParanoid

P35244.

KO

K10740.

OMA

TIMCASY.

OrthoDB

EOG4NVZMT.

PhylomeDB

P35244.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P35244.

Bgee

P35244.

CleanEx

HS_RPA3.

Genevestigator

P35244.

GermOnline

ENSG00000106399. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

InterPro

IPR012340. NA-bd_OB-fold.
IPR013970. Rep_factor-A_3.
[Graphical view]

Pfam

PF08661. Rep_fac-A_3. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RPA3. human.

EvolutionaryTrace

P35244.

GenomeRNAi

6119.

NextBio

23763.

SOURCE

Search...

Entry information

Entry name

RFA3_HUMAN

Accession

Primary (citable) accession number: P35244
Secondary accession number(s): Q549U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.