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Protein

Replication protein A 32 kDa subunit

Gene

RPA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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. 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. 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. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.13 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi74 – 148OBAdd BLAST75

<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

  • damaged DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: GO_Central
  • enzyme binding Source: UniProtKB
  • G-rich strand telomeric DNA binding Source: BHF-UCL
  • protein N-terminus binding Source: Ensembl
  • protein phosphatase binding Source: UniProtKB
  • sequence-specific DNA binding Source: GO_Central
  • single-stranded DNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA recombination, DNA repair, DNA replication

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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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

SIGNOR Signaling Network Open Resource

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SIGNORi
P15927

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Replication protein A 32 kDa subunit
Short name:
RP-A p32
Alternative name(s):
Replication factor A protein 2
Short name:
RF-A protein 2
Replication protein A 34 kDa subunit
Short name:
RP-A p34
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPA2
Synonyms:REPA2, RPA32, RPA34
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000117748.9

Human Gene Nomenclature Database

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HGNCi
HGNC:10290 RPA2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
179836 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P15927

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4S → A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-8. 1 Publication1
Mutagenesisi8S → A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-4. 2 Publications1
Mutagenesisi8S → D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-33. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-23; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-23; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-23; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-23; D-29 and D-33. 2 Publications1
Mutagenesisi23S → D: No effect on DNA synthesis following DNA damage; when associated with D-29. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-29 and D-33. 1 Publication1
Mutagenesisi29S → A: Reduces phosphorylation by CDK1. 2 Publications1
Mutagenesisi29S → D: No effect on DNA synthesis following DNA damage; when associated with D-23. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-33. 2 Publications1
Mutagenesisi33S → D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-8. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-29. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-29. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-29. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-29. 1 Publication1
Mutagenesisi37 – 38KK → RR: Impaired ubiquitination without affecting homologous recombination. 1 Publication2
Mutagenesisi248F → A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair. 1 Publication1
Mutagenesisi252E → A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair. 1 Publication1
Mutagenesisi253G → A: Does not affect interaction with RFWD3. 1 Publication1
Mutagenesisi254H → A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
6118

Open Targets

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OpenTargetsi
ENSG00000117748

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34652

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RPA2

Domain mapping of disease mutations (DMDM)

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DMDMi
132474

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000972701 – 270Replication protein A 32 kDa subunitAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4Phosphoserine; by PRKDC2 Publications1
Modified residuei8Phosphoserine; by PRKDC2 Publications1
Modified residuei21Phosphothreonine; by PRKDC4 Publications1
Modified residuei23Phosphoserine; by CDK2Combined sources3 Publications1
Modified residuei29Phosphoserine; by CDK1Combined sources4 Publications1
Modified residuei33Phosphoserine; by PRKDC3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence.9 Publications
DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR (PubMed:24332808). 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).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P15927

MaxQB - The MaxQuant DataBase

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MaxQBi
P15927

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P15927

PeptideAtlas

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PeptideAtlasi
P15927

PRoteomics IDEntifications database

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PRIDEi
P15927

ProteomicsDB human proteome resource

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ProteomicsDBi
53246
53247 [P15927-2]
53248 [P15927-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P15927

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P15927

SwissPalm database of S-palmitoylation events

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SwissPalmi
P15927

<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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Translationally up-regulated in response to DNA damage (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000117748 Expressed in 227 organ(s), highest expression level in leukocyte

CleanEx database of gene expression profiles

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CleanExi
HS_RPA2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P15927 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P15927 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB016538
HPA026306
HPA026309

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the replication protein A complex (RPA/RP-A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3 (PubMed:2406247, PubMed:19116208, PubMed:10449415). Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA) (PubMed:24332808). Interacts with SERTAD3 (PubMed:10982866). Interacts with TIPIN (PubMed:17141802, PubMed:17296725). Interacts with TIMELESS (PubMed:17141802). Interacts with PPP4R2; the interaction is direct, DNA damage-dependent and mediates the recruitment of the PP4 catalytic subunit PPP4C (PubMed:20154705). Interacts (hyperphosphorylated) with RAD51 (PubMed:20154705). Interacts with SMARCAL1; the interaction is direct and mediates the recruitment to the RPA complex of SMARCAL1 (PubMed:19793861, PubMed:19793862, PubMed:19793863). Interacts with RAD52 and XPA; those interactions are direct and associate RAD52 and XPA to the RPA complex (PubMed:7700386, PubMed:8702565, PubMed:17765923, PubMed:11081631). Interacts with FBH1 (PubMed:23319600). Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks (PubMed:27601467, PubMed:27723720, PubMed:27723717). Interacts with RFWD3 (PubMed:21504906, PubMed:21558276, PubMed:26474068, PubMed:28575657).22 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112038, 462 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P15927

Database of interacting proteins

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DIPi
DIP-24187N

Protein interaction database and analysis system

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IntActi
P15927, 90 interactors

Molecular INTeraction database

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MINTi
P15927

STRING: functional protein association networks

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STRINGi
9606.ENSP00000363021

<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

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P15927

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P15927

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P15927

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni187 – 270Interaction with RAD52, TIPIN, UNG and XPA1 PublicationAdd BLAST84

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 29Gly/Ser-richAdd BLAST29
Compositional biasi37 – 45Arg/Lys-rich (basic)9
Compositional biasi95 – 123Asp/Glu-rich (acidic)Add BLAST29
Compositional biasi127 – 145Arg/Lys-rich (basic)Add BLAST19
Compositional biasi247 – 270Asp/Glu-rich (acidic)Add BLAST24

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3108 Eukaryota
COG5235 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000010045

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000216562

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000086

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15927

KEGG Orthology (KO)

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KOi
K10739

Identification of Orthologs from Complete Genome Data

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OMAi
EATYVHL

Database of Orthologous Groups

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OrthoDBi
EOG091G0L35

Database for complete collections of gene phylogenies

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PhylomeDBi
P15927

TreeFam database of animal gene trees

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TreeFami
TF105242

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR012340 NA-bd_OB-fold
IPR040260 RFA2-like
IPR014646 Rfa2/RPA32
IPR014892 RPA_C
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

The PANTHER Classification System

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PANTHERi
PTHR13989 PTHR13989, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08784 RPA_C, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF036949 RPA32, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46785 SSF46785, 1 hit
SSF50249 SSF50249, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P15927-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT
60 70 80 90 100
ISQLLSATLV DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA
110 120 130 140 150
PMDVRQWVDT DDTSSENTVV PPETYVKVAG HLRSFQNKKS LVAFKIMPLE
160 170 180 190 200
DMNEFTTHIL EVINAHMVLS KANSQPSAGR APISNPGMSE AGNFGGNSFM
210 220 230 240 250
PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS SIKQAVDFLS
260 270
NEGHIYSTVD DDHFKSTDAE
Length:270
Mass (Da):29,247
Last modified:April 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i61A563EA7B34A9B1
GO
Isoform 2 (identifier: P15927-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MWNS → MGRGDRNKRSIR

Note: No experimental confirmation available.
Show »
Length:278
Mass (Da):30,156
Checksum:i680A88DB44410EBC
GO
Isoform 3 (identifier: P15927-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MWNS → MWNSNDGGAG...QALILLFKTG

Note: No experimental confirmation available.
Show »
Length:358
Mass (Da):38,810
Checksum:iB21291661BDEEAFA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5TEJ0Q5TEJ0_HUMAN
Replication protein A 32 kDa subuni...
RPA2
122Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5TEJ7Q5TEJ7_HUMAN
Replication protein A 32 kDa subuni...
RPA2
179Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02330014Y → S1 PublicationCorresponds to variant dbSNP:rs28988896Ensembl.1
Natural variantiVAR_02330115G → R1 PublicationCorresponds to variant dbSNP:rs28988897Ensembl.1
Natural variantiVAR_023302203N → S1 PublicationCorresponds to variant dbSNP:rs28904899Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0172011 – 4MWNS → MGRGDRNKRSIR in isoform 2. Curated4
Alternative sequenceiVSP_0172021 – 4MWNS → MWNSNDGGAGWRRKRIAGGF SKRASLGSERRVVAGEEGRE RSWGVWGSPAGRRRGRLGRL GQCLKGRSLREPAGFSEAWD VAQALILLFKTG in isoform 3. Curated4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J05249 mRNA Translation: AAA36560.1
CR450348 mRNA Translation: CAG29344.1
DQ001128 Genomic DNA Translation: AAX84514.1
AL109927 Genomic DNA No translation available.
BC001630 mRNA Translation: AAH01630.1
BC012157 mRNA Translation: AAH12157.1
BC021257 mRNA Translation: AAH21257.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS314.1 [P15927-1]
CCDS72740.1 [P15927-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A43711

NCBI Reference Sequences

More...
RefSeqi
NP_001273005.1, NM_001286076.1
NP_001284487.1, NM_001297558.1 [P15927-2]
NP_002937.1, NM_002946.4 [P15927-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.79411

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000313433; ENSP00000363015; ENSG00000117748 [P15927-3]
ENST00000373909; ENSP00000363017; ENSG00000117748 [P15927-2]
ENST00000373912; ENSP00000363021; ENSG00000117748 [P15927-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6118

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6118

UCSC genome browser

More...
UCSCi
uc001bpe.3 human [P15927-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05249 mRNA Translation: AAA36560.1
CR450348 mRNA Translation: CAG29344.1
DQ001128 Genomic DNA Translation: AAX84514.1
AL109927 Genomic DNA No translation available.
BC001630 mRNA Translation: AAH01630.1
BC012157 mRNA Translation: AAH12157.1
BC021257 mRNA Translation: AAH21257.1
CCDSiCCDS314.1 [P15927-1]
CCDS72740.1 [P15927-2]
PIRiA43711
RefSeqiNP_001273005.1, NM_001286076.1
NP_001284487.1, NM_001297558.1 [P15927-2]
NP_002937.1, NM_002946.4 [P15927-1]
UniGeneiHs.79411

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 entryMethodResolution (Å)ChainPositionsPDBsum
1DPUNMR-A172-270[»]
1L1OX-ray2.80B/E44-171[»]
1QUQX-ray2.50A/C43-171[»]
1Z1DNMR-A172-270[»]
2PI2X-ray2.00A/B/C/D1-270[»]
2PQAX-ray2.50A/C42-172[»]
2Z6KX-ray3.00A/B1-270[»]
3KDFX-ray1.98B/D41-172[»]
4MQVX-ray1.95A/C202-270[»]
4OU0X-ray1.40A202-270[»]
ProteinModelPortaliP15927
SMRiP15927
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112038, 462 interactors
CORUMiP15927
DIPiDIP-24187N
IntActiP15927, 90 interactors
MINTiP15927
STRINGi9606.ENSP00000363021

PTM databases

iPTMnetiP15927
PhosphoSitePlusiP15927
SwissPalmiP15927

Polymorphism and mutation databases

BioMutaiRPA2
DMDMi132474

Proteomic databases

EPDiP15927
MaxQBiP15927
PaxDbiP15927
PeptideAtlasiP15927
PRIDEiP15927
ProteomicsDBi53246
53247 [P15927-2]
53248 [P15927-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6118
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313433; ENSP00000363015; ENSG00000117748 [P15927-3]
ENST00000373909; ENSP00000363017; ENSG00000117748 [P15927-2]
ENST00000373912; ENSP00000363021; ENSG00000117748 [P15927-1]
GeneIDi6118
KEGGihsa:6118
UCSCiuc001bpe.3 human [P15927-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6118
DisGeNETi6118
EuPathDBiHostDB:ENSG00000117748.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RPA2
HGNCiHGNC:10290 RPA2
HPAiCAB016538
HPA026306
HPA026309
MIMi179836 gene
neXtProtiNX_P15927
OpenTargetsiENSG00000117748
PharmGKBiPA34652

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3108 Eukaryota
COG5235 LUCA
GeneTreeiENSGT00390000010045
HOGENOMiHOG000216562
HOVERGENiHBG000086
InParanoidiP15927
KOiK10739
OMAiEATYVHL
OrthoDBiEOG091G0L35
PhylomeDBiP15927
TreeFamiTF105242

Enzyme and pathway databases

ReactomeiR-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
SIGNORiP15927

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RPA2 human
EvolutionaryTraceiP15927

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RPA2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6118

Protein Ontology

More...
PROi
PR:P15927

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000117748 Expressed in 227 organ(s), highest expression level in leukocyte
CleanExiHS_RPA2
ExpressionAtlasiP15927 baseline and differential
GenevisibleiP15927 HS

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR040260 RFA2-like
IPR014646 Rfa2/RPA32
IPR014892 RPA_C
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR13989 PTHR13989, 1 hit
PfamiView protein in Pfam
PF08784 RPA_C, 1 hit
PIRSFiPIRSF036949 RPA32, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF50249 SSF50249, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRFA2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15927
Secondary accession number(s): Q52II0, Q5TEI9, Q5TEJ5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 5, 2018
This is version 202 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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