P27694 (RFA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

General annotation (Comments)

Function	Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing. Ref.16 Ref.18 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.16 Ref.18
Subunit structure	Heterotrimer composed of RPA1, RPA2 and RPA3 (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 RPA1 subunit. Interacts with RIPK1 and XPA. Interacts with RPA4. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 Ref.22
Subcellular location	Nucleus.
Post-translational modification	Sumoylated on lysine residues Lys-449 and Lys-577, with Lys-449 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6. Ref.19
Sequence similarities	Belongs to the replication factor A protein 1 family.
Sequence caution	The sequence BAD92969.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing 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 hemopoiesis Inferred from electronic annotation. Source: Compara homeostasis of number of cells within a tissue Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara meiosis Inferred from electronic annotation. Source: Compara nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara 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 Inferred from physical interaction Ref.13. Source: MGI PML body Inferred from direct assay Ref.13. Source: MGI actin cytoskeleton Inferred from direct assay. Source: HPA cytoplasm Inferred from direct assay. Source: HPA lateral element Inferred from electronic annotation. Source: Compara male germ cell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Traceable author statement PubMed 8756712. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLM	P54132	3	EBI-621389,EBI-621372
RPA2	P15927	4	EBI-621389,EBI-621404
RPA3	P35244	4	EBI-621389,EBI-621428
WRN	Q14191	8	EBI-621389,EBI-368417

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 616

615

Replication protein A 70 kDa DNA-binding subunit

PRO_0000097260

Regions

Zinc finger

481 – 503

23

C4-type Potential

Amino acid modifications

Modified residue

163

1

N6-acetyllysine Ref.17

Modified residue

167

1

N6-acetyllysine Ref.17

Modified residue

180

1

Phosphothreonine Ref.14 Ref.20

Modified residue

191

1

Phosphothreonine Ref.20

Modified residue

259

1

N6-acetyllysine Ref.17

Modified residue

384

1

Phosphoserine Ref.20

Cross-link

449

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19

Cross-link

577

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19

Natural variations

Natural variant

351

1

T → A. Ref.4 Ref.5
Corresponds to variant rs5030755 [ dbSNP | Ensembl ].

VAR_019236

Experimental info

Mutagenesis

41

1

R → E: Loss of HELB-binding; when associated with E-43. Ref.22

Mutagenesis

43

1

R → E: Loss of HELB-binding; when associated with E-41. Ref.22

Mutagenesis

449

1

K → R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577. Ref.19

Mutagenesis

577

1

K → R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449. Ref.19

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

616

Helix Strand Turn

Details...

Helix

2 – 4

3

Helix

9 – 16

8

Beta strand

18 – 20

3

Beta strand

24 – 33

10

Beta strand

36 – 38

3

Beta strand

41 – 47

7

Beta strand

49 – 58

10

Helix

60 – 62

3

Helix

63 – 67

5

Beta strand

70 – 74

5

Beta strand

76 – 86

11

Beta strand

88 – 90

3

Beta strand

92 – 103

12

Helix

105 – 108

4

Helix

187 – 189

3

Beta strand

198 – 206

9

Beta strand

210 – 213

4

Beta strand

218 – 227

10

Beta strand

232 – 238

7

Helix

239 – 245

7

Helix

246 – 248

3

Beta strand

254 – 258

5

Beta strand

261 – 264

4

Helix

267 – 269

3

Beta strand

275 – 279

5

Beta strand

285 – 288

4

Helix

305 – 310

6

Beta strand

316 – 326

11

Beta strand

330 – 334

5

Turn

335 – 338

4

Beta strand

339 – 349

11

Beta strand

355 – 361

7

Helix

362 – 367

6

Beta strand

375 – 384

10

Beta strand

388 – 392

5

Beta strand

398 – 402

5

Helix

406 – 416

11

Turn

417 – 419

3

Helix

445 – 451

7

Turn

452 – 454

3

Beta strand

455 – 458

4

Beta strand

460 – 471

12

Beta strand

477 – 480

4

Beta strand

491 – 493

3

Turn

494 – 496

3

Beta strand

497 – 500

4

Turn

501 – 504

4

Beta strand

505 – 509

5

Beta strand

512 – 521

10

Beta strand

526 – 532

7

Helix

533 – 540

8

Helix

544 – 550

7

Helix

555 – 564

10

Turn

565 – 567

3

Beta strand

569 – 577

9

Beta strand

588 – 596

9

Helix

599 – 615

17

Sequences

	Sequence		Length	Mass (Da)
	P27694 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: FE038F40F5886CD1	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

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 217.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	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.
[5]	NIEHS SNPs program Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-351.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Uterus.
[8]	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.
[9]	"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.
[10]	"Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms." Braun K.A., Lao Y., He Z., Ingles C.J., Wold M.S. Biochemistry 36:8443-8454(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POLA1.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XPA.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XPA.
[13]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIPK1.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-167 AND LYS-259, MASS SPECTROMETRY.
[18]	"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.
[19]	"Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex." Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T. Mol. Cell 39:333-345(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-449 AND LYS-577, DESUMOYLATION BY SENP6, MUTAGENESIS OF LYS-449 AND LYS-577, INTERACTION WITH SENP6 AND RAD51.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180; THR-191 AND SER-384, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress." Guler G.D., Liu H., Vaithiyalingam S., Arnett D.R., Kremmer E., Chazin W.J., Fanning E. J. Biol. Chem. 287:6469-6481(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HELB, MUTAGENESIS OF ARG-41 AND ARG-43.
[23]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63488 mRNA. Translation: AAA36584.1.
AK289704 mRNA. Translation: BAF82393.1.
AB209732 mRNA. Translation: BAD92969.1. Different initiation.
AY599563 Genomic DNA. Translation: AAS94324.1.
CH471108 Genomic DNA. Translation: EAW90574.1.
BC018126 mRNA. Translation: AAH18126.1.

IPI

IPI00020127.

PIR

A40457.

RefSeq

NP_002936.1. NM_002945.3.

UniGene

Hs.461925.

3D structure databases

PDBe
RCSB PDB
PDBj

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.

ProteinModelPortal

P27694.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24189N.

IntAct

P27694. 32 interactions.

MINT

MINT-91488.

STRING

9606.ENSP00000254719.

PTM databases

PhosphoSite

P27694.

Polymorphism databases

DMDM

1350579.

Proteomic databases

PaxDb

P27694.

PeptideAtlas

P27694.

PRIDE

P27694.

Protocols and materials databases

DNASU

6117.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254719; ENSP00000254719; ENSG00000132383.

GeneID

6117.

KEGG

hsa:6117.

UCSC

uc002fto.2. human.

Organism-specific databases

CTD

6117.

GeneCards

GC17P001680.

HGNC

HGNC:10289. RPA1.

HPA

CAB004563.
HPA006914.

MIM

179835. gene.

neXtProt

NX_P27694.

PharmGKB

PA34651.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1599.

HOGENOM

HOG000162322.

HOVERGEN

HBG010502.

InParanoid

P27694.

KO

K07466.

OMA

QNKWVIK.

OrthoDB

EOG4V9TQ8.

PhylomeDB

P27694.

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

P27694.

Bgee

P27694.

CleanEx

HS_RPA1.

Genevestigator

P27694.

GermOnline

ENSG00000132383. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 4 hits.

InterPro

IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA-helicase.
IPR013955. Rep_factor-A_C.
IPR007199. Rep_factor-A_N.
IPR004591. Rep_factor_Rpa1.
[Graphical view]

Pfam

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

SUPFAM

SSF50249. Nucleic_acid_OB. 4 hits.

TIGRFAMs

TIGR00617. rpa1. 1 hit.

ProtoNet

Search...

Other

BindingDB

P27694.

ChEMBL

CHEMBL1764940.

ChiTaRS

RPA1. human.

EvolutionaryTrace

P27694.

GenomeRNAi

6117.

NextBio

23755.

SOURCE

Search...

Entry information

Entry name

RFA1_HUMAN

Accession

Primary (citable) accession number: P27694
Secondary accession number(s): A8K0Y9, Q59ES9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 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.