Replication protein A 70 kDa DNA-binding subunit

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Reviewed, UniProtKB/Swiss-Prot P27694 (RFA1_HUMAN)

Last modified June 16, 2009. Version 100. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	616 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	It participates in a very early step in initiation. RP-A is a single-stranded DNA-binding protein. Absolutely required for simian virus 40 DNA replication in vitro.
Subunit structure	Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding activity may reside exclusively on the 70 kDa subunit. Interacts with RIP and XPA. Interacts with RPA4. Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12
Sequence similarities	Belongs to the replication factor A protein 1 family.

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Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA-dependent DNA replication Traceable author statement. Source: ProtInc 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.10 Inferred from physical interaction. Source: MGI PML body Ref.10 Inferred from direct assay. Source: MGI cytoplasm Inferred from direct assay. Source: HPA cytoskeleton Inferred from direct assay. Source: HPA
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB single-stranded DNA binding Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
BLM	P54132	1	EBI-621389,EBI-621372
TP53	P04637	1	EBI-621389,EBI-366083
WRN	Q14191	4	EBI-621389,EBI-368417

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 616

615

Replication protein A 70 kDa DNA-binding subunit

PRO_0000097260

Regions

Zinc finger

481 – 503

C4-type Potential

Amino acid modifications

Modified residue

180

Phosphothreonine Ref.11

Modified residue

384

Phosphoserine Ref.12

Natural variations

Natural variant

351

T → A: dbSNP rs5030755. Ref.3 Ref.4

VAR_019236

Secondary structure

616

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P27694-1 [UniParc].

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

616

68,138

        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

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References

	« Hide 'large scale' referencesShow '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: 2050703] [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: 8420996] [Abstract] Cited for: SEQUENCE REVISION TO 217.
[3]	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.
[4]	NIEHS SNPs program Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-351.
[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: Uterus.
[6]	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, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[7]	"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.
[8]	"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: 9699634] [Abstract] Cited for: INTERACTION WITH XPA.
[9]	"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: 10563794] [Abstract] Cited for: INTERACTION WITH XPA.
[10]	"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: 16135809] [Abstract] Cited for: INTERACTION WITH RIP.
[11]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, MASS SPECTROMETRY.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 8990123] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

M63488 mRNA. Translation: AAA36584.1.
AB209732 mRNA. Translation: BAD92969.1. Different initiation.
AY599563 Genomic DNA. Translation: AAS94324.1.
BC018126 mRNA. Translation: AAH18126.1.

IPI

IPI00020127.

PIR

A40457.

RefSeq

NP_002936.1.

UniGene

Hs.461925
Hs.595562

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EWI	NMR	-	A	1-114	[»]
1FGU	X-ray	2.50	A/B	182-432	[»]
1JMC	X-ray	2.40	A	181-422	[»]
1L1O	X-ray	2.80	C/F	436-616	[»]
2B29	X-ray	1.60	A	1-120	[»]
2B3G	X-ray	1.60	A	1-120	[»]

DisProt

DP00061.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:24189N.

IntAct

P27694. 16 interactions.

PTM databases

PhosphoSite

P27694.

Proteomic databases

PeptideAtlas

P27694.

PRIDE

P27694.

Genome annotation databases

Ensembl

ENSG00000132383. Homo sapiens. [Contig view]

GeneID

6117.

KEGG

hsa:6117.

Organism-specific databases

GeneCards

GC17P001680.

H-InvDB

HIX0017624.

HGNC

HGNC:10289. RPA1.

HPA

CAB004563.
HPA006914.

MIM

179835. gene.

PharmGKB

PA29353.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P27694.

HOVERGEN

P27694.

OMA

P27694. TLWGEDA.

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

P27694.

Bgee

P27694.

CleanEx

HS_RPA1.

GermOnline

ENSG00000132383. Homo sapiens.

Family and domain databases

InterPro

IPR012340. NA-bd_OB-fold.
IPR004365. NA_bd_OB_tRNA-helicase.
IPR007199. Rep-A_N.
IPR013955. Rep_factor-A_C.
IPR004591. Rpa1.
[Graphical view]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 4 hits.

Pfam

PF04057. Rep-A_N. 1 hit.
PF08646. Rep_fac-A_C. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00617. rpa1. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

23755.

SOURCE

Search...

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Entry information

Entry name

RFA1_HUMAN

Accession

Primary (citable) accession number: P27694
Secondary accession number(s): Q59ES9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents