RPA3

Functionⁱ

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).1 Publication6 Publications

GO - Molecular functionⁱ

damaged DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 7700386
single-stranded DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19010961

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

base-excision repair
Source: UniProtKB
Inferred from direct assayⁱ
- 9765279
DNA damage response, detection of DNA damage Source: Reactome
DNA replication
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9430682
double-strand break repair via homologous recombination
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17765923
error-free translesion synthesis Source: Reactome
error-prone translesion synthesis Source: Reactome
G1/S transition of mitotic cell cycle Source: Reactome
interstrand cross-link repair Source: Reactome
mismatch repair
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9430682
nucleotide-excision repair
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9430682
nucleotide-excision repair, DNA gap filling Source: Reactome
nucleotide-excision repair, DNA incision Source: Reactome
nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
nucleotide-excision repair, preincision complex assembly Source: Reactome
nucleotide-excision repair, preincision complex stabilization Source: Reactome
regulation of cell proliferation Source: Ensembl
regulation of cellular response to heat Source: Reactome
regulation of mitotic cell cycle Source: Ensembl
telomere maintenance
Source: BHF-UCL
Traceable author statementⁱ
- 24747047
telomere maintenance via semi-conservative replication Source: Reactome
transcription-coupled nucleotide-excision repair Source: Reactome
translesion synthesis Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	DNA damage, DNA recombination, DNA repair, DNA replication

Biological process

DNA damage, DNA recombination, DNA repair, DNA replication

Enzyme and pathway databases

Reactomeⁱ	R-HSA-110312 Translesion synthesis by REV1 R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex R-HSA-110320 Translesion Synthesis by POLH R-HSA-174437 Removal of the Flap Intermediate from the C-strand R-HSA-176187 Activation of ATR in response to replication stress R-HSA-3371453 Regulation of HSF1-mediated heat shock response R-HSA-3371511 HSF1 activation R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair R-HSA-5655862 Translesion synthesis by POLK R-HSA-5656121 Translesion synthesis by POLI R-HSA-5656169 Termination of translesion DNA synthesis R-HSA-5685938 HDR through Single Strand Annealing (SSA) R-HSA-5685942 HDR through Homologous Recombination (HRR) R-HSA-5693607 Processing of DNA double-strand break ends R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER R-HSA-5696400 Dual Incision in GG-NER R-HSA-6782135 Dual incision in TC-NER R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-6783310 Fanconi Anemia Pathway R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation R-HSA-68962 Activation of the pre-replicative complex R-HSA-69166 Removal of the Flap Intermediate R-HSA-69473 G2/M DNA damage checkpoint R-HSA-912446 Meiotic recombination

Reactomeⁱ

R-HSA-110312 Translesion synthesis by REV1
R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320 Translesion Synthesis by POLH
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-176187 Activation of ATR in response to replication stress
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371511 HSF1 activation
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5655862 Translesion synthesis by POLK
R-HSA-5656121 Translesion synthesis by POLI
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6783310 Fanconi Anemia Pathway
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-68962 Activation of the pre-replicative complex
R-HSA-69166 Removal of the Flap Intermediate
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-912446 Meiotic recombination

Names & Taxonomyⁱ

Protein namesⁱ	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 namesⁱ	Name:RPA3 Synonyms:REPA3, RPA14
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 7

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000106399.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10291 RPA3
MIMⁱ	179837 gene
neXtProtⁱ	NX_P35244

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6119
Open Targets More...OpenTargetsⁱ	ENSG00000106399
PharmGKBⁱ	PA34653

Polymorphism and mutation databases

BioMutaⁱ	RPA3
DMDMⁱ	464608

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000097276	2 – 121	Replication protein A 14 kDa subunitAdd BLAST		120

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylvalineCombined sources	1
Cross-linkⁱ	23	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	39	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	88	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationⁱ

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).1 Publication

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDⁱ	P35244
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P35244
PaxDbⁱ	P35244
PeptideAtlas More...PeptideAtlasⁱ	P35244
PRIDEⁱ	P35244
ProteomicsDBⁱ	55011
TopDownProteomicsⁱ	P35244

PTM databases

iPTMnetⁱ	P35244
PhosphoSitePlusⁱ	P35244

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000106399 Expressed in 225 organ(s), highest expression level in bronchial epithelial cell
CleanExⁱ	HS_RPA3
ExpressionAtlasⁱ	P35244 baseline and differential
Genevisibleⁱ	P35244 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA005708

HPAⁱ

HPA005708

Interactionⁱ

Subunit structureⁱ

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 RPA2.2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
RAD52	P43351	3	EBI-621428,EBI-706448
RPA1	P27694	8	EBI-621428,EBI-621389
RPA2	P15927	8	EBI-621428,EBI-621404

Protein-protein interaction databases

BioGridⁱ	112039, 397 interactors
CORUMⁱ	P35244
Database of interacting proteins More...DIPⁱ	DIP-24190N
IntActⁱ	P35244, 38 interactors
Molecular INTeraction database More...MINTⁱ	P35244
STRINGⁱ	9606.ENSP00000223129

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 6	Combined sources	3
Beta strandⁱ	10 – 12	Combined sources	3
Helixⁱ	14 – 20	Combined sources	7
Beta strandⁱ	24 – 34	Combined sources	11
Beta strandⁱ	38 – 44	Combined sources	7
Beta strandⁱ	50 – 54	Combined sources	5
Beta strandⁱ	65 – 73	Combined sources	9
Beta strandⁱ	79 – 86	Combined sources	8
Beta strandⁱ	90 – 92	Combined sources	3
Helixⁱ	96 – 108	Combined sources	13
Helixⁱ	110 – 112	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P35244
SMRⁱ	P35244
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P35244

EvolutionaryTraceⁱ

P35244

Family & Domainsⁱ

Phylogenomic databases

eggNOGⁱ	ENOG410IZRM Eukaryota ENOG4111REI LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008029
HOGENOMⁱ	HOG000252930
HOVERGENⁱ	HBG003004
InParanoidⁱ	P35244
KEGG Orthology (KO) More...KOⁱ	K10740
OMAⁱ	KPRINCS
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G1178
PhylomeDBⁱ	P35244
TreeFamⁱ	TF105243

Family and domain databases

InterProⁱ	View protein in InterPro IPR012340 NA-bd_OB-fold IPR013970 Rfa2
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08661 Rep_fac-A_3, 1 hit
SUPFAMⁱ	SSF50249 SSF50249, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P35244-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN 
        60         70         80         90        100
GTIELMEPLD EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN 
       110        120 
EAVKIIHDFP QFYPLGIVQH D

Length:121

Mass (Da):13,569

Last modified:February 1, 1994 - v1

Checksum:ⁱ3FD99851959FB498

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	B5MC59	B5MC59_HUMAN		Replication protein A 14 kDa subuni... Replication protein A 14 kDa subunit (Replication protein A3, 14kDa, isoform CRA_a)	RPA3 hCG_17407	82	Annotation score:

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS5356.1
PIRⁱ	A46008
NCBI Reference Sequences More...RefSeqⁱ	NP_002938.1, NM_002947.4
UniGeneⁱ	Hs.487540

Genome annotation databases

Ensemblⁱ	ENST00000223129; ENSP00000223129; ENSG00000106399 ENST00000396682; ENSP00000379914; ENSG00000106399
GeneIDⁱ	6119
KEGGⁱ	hsa:6119
UCSC genome browser More...UCSCⁱ	uc003sri.4 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P35244	Replication protein A3, 14kDa		HUMAN		121	UniRef100_P35244
Replication protein A 14 kDa subunit		HUMAN		82
UPI0001753D82		HUMAN		142

Protein	Similar proteins		Species	Score	Length	Source
P35244	Replication protein A3, 14kDa		HUMAN		121	UniRef90_P35244
Uncharacterized protein		PAPAN		121
Replication protein A 14 kDa subunit		MACMU		121
Uncharacterized protein		CERAT		121
Uncharacterized protein		MANLE		121
+25

Protein	Similar proteins		Species	Score	Length	Source
P35244	Replication protein A3, 14kDa		HUMAN		121	UniRef50_P35244
Uncharacterized protein		NOMLE		121
Replication protein A 14 kDa subunit		CASCN		121
Uncharacterized protein		CHLSB		121
Uncharacterized protein		PAPAN		121
+43

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
CCDSⁱ	CCDS5356.1
PIRⁱ	A46008
RefSeqⁱ	NP_002938.1, NM_002947.4
UniGeneⁱ	Hs.487540

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	1-121	[»]
ProteinModelPortalⁱ	P35244
SMRⁱ	P35244
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	112039, 397 interactors
CORUMⁱ	P35244
DIPⁱ	DIP-24190N
IntActⁱ	P35244, 38 interactors
MINTⁱ	P35244
STRINGⁱ	9606.ENSP00000223129

PTM databases

iPTMnetⁱ	P35244
PhosphoSitePlusⁱ	P35244

Polymorphism and mutation databases

BioMutaⁱ	RPA3
DMDMⁱ	464608

Proteomic databases

EPDⁱ	P35244
MaxQBⁱ	P35244
PaxDbⁱ	P35244
PeptideAtlasⁱ	P35244
PRIDEⁱ	P35244
ProteomicsDBⁱ	55011
TopDownProteomicsⁱ	P35244

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	6119
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000223129; ENSP00000223129; ENSG00000106399 ENST00000396682; ENSP00000379914; ENSG00000106399
GeneIDⁱ	6119
KEGGⁱ	hsa:6119
UCSCⁱ	uc003sri.4 human

Organism-specific databases

CTDⁱ	6119
DisGeNETⁱ	6119
EuPathDBⁱ	HostDB:ENSG00000106399.11
GeneCardsⁱ	RPA3
HGNCⁱ	HGNC:10291 RPA3
HPAⁱ	HPA005708
MIMⁱ	179837 gene
neXtProtⁱ	NX_P35244
OpenTargetsⁱ	ENSG00000106399
PharmGKBⁱ	PA34653
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IZRM Eukaryota ENOG4111REI LUCA
GeneTreeⁱ	ENSGT00390000008029
HOGENOMⁱ	HOG000252930
HOVERGENⁱ	HBG003004
InParanoidⁱ	P35244
KOⁱ	K10740
OMAⁱ	KPRINCS
OrthoDBⁱ	EOG091G1178
PhylomeDBⁱ	P35244
TreeFamⁱ	TF105243

Enzyme and pathway databases

Reactomeⁱ	R-HSA-110312 Translesion synthesis by REV1 R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex R-HSA-110320 Translesion Synthesis by POLH R-HSA-174437 Removal of the Flap Intermediate from the C-strand R-HSA-176187 Activation of ATR in response to replication stress R-HSA-3371453 Regulation of HSF1-mediated heat shock response R-HSA-3371511 HSF1 activation R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair R-HSA-5655862 Translesion synthesis by POLK R-HSA-5656121 Translesion synthesis by POLI R-HSA-5656169 Termination of translesion DNA synthesis R-HSA-5685938 HDR through Single Strand Annealing (SSA) R-HSA-5685942 HDR through Homologous Recombination (HRR) R-HSA-5693607 Processing of DNA double-strand break ends R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER R-HSA-5696400 Dual Incision in GG-NER R-HSA-6782135 Dual incision in TC-NER R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-6783310 Fanconi Anemia Pathway R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation R-HSA-68962 Activation of the pre-replicative complex R-HSA-69166 Removal of the Flap Intermediate R-HSA-69473 G2/M DNA damage checkpoint R-HSA-912446 Meiotic recombination

Reactomeⁱ

R-HSA-110312 Translesion synthesis by REV1
R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320 Translesion Synthesis by POLH
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-176187 Activation of ATR in response to replication stress
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371511 HSF1 activation
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5655862 Translesion synthesis by POLK
R-HSA-5656121 Translesion synthesis by POLI
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6783310 Fanconi Anemia Pathway
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-68962 Activation of the pre-replicative complex
R-HSA-69166 Removal of the Flap Intermediate
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-912446 Meiotic recombination

Miscellaneous databases

ChiTaRSⁱ	RPA3 human
EvolutionaryTraceⁱ	P35244
GeneWikiⁱ	RPA3
GenomeRNAiⁱ	6119
Protein Ontology More...PROⁱ	PR:P35244
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000106399 Expressed in 225 organ(s), highest expression level in bronchial epithelial cell
CleanExⁱ	HS_RPA3
ExpressionAtlasⁱ	P35244 baseline and differential
Genevisibleⁱ	P35244 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR012340 NA-bd_OB-fold IPR013970 Rfa2
Pfamⁱ	View protein in Pfam PF08661 Rep_fac-A_3, 1 hit
SUPFAMⁱ	SSF50249 SSF50249, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RFA3_HUMAN
Accessionⁱ	P35244Primary (citable) accession number: P35244 Secondary accession number(s): Q549U6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
	Last sequence update:	February 1, 1994
	Last modified:	October 10, 2018
	This is version 174 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P35244 (RFA3_HUMAN)

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Replication protein A 14 kDa subunit

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ