Reviewed, UniProtKB/Swiss-Prot P35244 (RFA3_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding activity may reside exclusively on the 70 kDa subunit. Interacts with RPA4. Ref.6
Subcellular location	Nucleus.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA replication Ref.1 Inferred from Experiment. Source: Reactome nucleotide-excision repair, DNA damage removal Inferred from Experiment. Source: Reactome nucleotide-excision repair, DNA gap filling Inferred from Experiment. Source: Reactome
Cellular component	DNA replication factor A complex Ref.1 Traceable author statement. Source: ProtInc cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	single-stranded DNA binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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

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121

Helix Strand Turn

Details...

Helix

4 – 6

3

Beta strand

10 – 12

3

Helix

14 – 19

6

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)
	P35244-1 [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: 8454588] [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: 12853948] [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: 15489334] [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: 7760808] [Abstract] Cited for: INTERACTION WITH RPA4.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"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: 11927569] [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

EMBLGenBankDDBJ

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.

UniGene

Hs.487540

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:24190N.

IntAct

P35244. 3 interactions.

Proteomic databases

PeptideAtlas

P35244.

PRIDE

P35244.

Genome annotation databases

Ensembl

ENSG00000106399. Homo sapiens. [Contig view]

GeneID

6119.

KEGG

hsa:6119.

Organism-specific databases

GeneCards

GC07M007643.

H-InvDB

HIX0017394.
HIX0057108.

HGNC

HGNC:10291. RPA3.

HPA

HPA005708.

MIM

179837. gene.

PharmGKB

PA29357.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P35244.

HOVERGEN

P35244.

OMA

P35244. TIMCASY.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_216. DNA Repair.
REACT_383. DNA Replication.
REACT_7970. Telomere Maintenance.

Gene expression databases

ArrayExpress

P35244.

Bgee

P35244.

CleanEx

HS_RPA3.

GermOnline

ENSG00000106399. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.

Pfam

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

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)