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P40938

- RFC3_HUMAN

UniProt

P40938 - RFC3_HUMAN

Protein

Replication factor C subunit 3

Gene

RFC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1.

    GO - Molecular functioni

    1. DNA clamp loader activity Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA repair Source: Reactome
    3. DNA replication Source: UniProtKB
    4. DNA strand elongation involved in DNA replication Source: Reactome
    5. DNA synthesis involved in DNA repair Source: UniProtKB
    6. mitotic cell cycle Source: Reactome
    7. nucleotide-excision repair Source: Reactome
    8. nucleotide-excision repair, DNA gap filling Source: Reactome
    9. response to organophosphorus Source: UniProtKB
    10. telomere maintenance Source: Reactome
    11. telomere maintenance via recombination Source: Reactome
    12. telomere maintenance via semi-conservative replication Source: Reactome
    13. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1792. Polymerase switching.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_7987. Polymerase switching on the C-strand of the telomere.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replication factor C subunit 3
    Alternative name(s):
    Activator 1 38 kDa subunit
    Short name:
    A1 38 kDa subunit
    Activator 1 subunit 3
    Replication factor C 38 kDa subunit
    Short name:
    RF-C 38 kDa subunit
    Short name:
    RFC38
    Gene namesi
    Name:RFC3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:9971. RFC3.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. DNA replication factor C complex Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34340.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356Replication factor C subunit 3PRO_0000121761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201N6-acetyllysine1 Publication
    Modified residuei125 – 1251Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP40938.
    PaxDbiP40938.
    PeptideAtlasiP40938.
    PRIDEiP40938.

    PTM databases

    PhosphoSiteiP40938.

    Expressioni

    Gene expression databases

    BgeeiP40938.
    CleanExiHS_RFC3.
    GenevestigatoriP40938.

    Organism-specific databases

    HPAiHPA030149.

    Interactioni

    Subunit structurei

    Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RFC4P352495EBI-1055010,EBI-476655

    Protein-protein interaction databases

    BioGridi111915. 29 interactions.
    DIPiDIP-36432N.
    IntActiP40938. 13 interactions.
    MINTiMINT-3015032.
    STRINGi9606.ENSP00000369411.

    Structurei

    3D structure databases

    ProteinModelPortaliP40938.
    SMRiP40938. Positions 4-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the activator 1 small subunits family.Curated

    Phylogenomic databases

    eggNOGiCOG0470.
    HOGENOMiHOG000224153.
    HOVERGENiHBG040509.
    InParanoidiP40938.
    KOiK10756.
    OMAiTRIMCLL.
    OrthoDBiEOG7FXZZD.
    PhylomeDBiP40938.
    TreeFamiTF105724.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR008921. DNA_pol3_clamp-load_cplx_C.
    IPR027417. P-loop_NTPase.
    IPR013748. Rep_factorC_C_dom.
    [Graphical view]
    PfamiPF08542. Rep_fac_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF48019. SSF48019. 1 hit.
    SSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P40938-1) [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.

    « Hide

    MSLWVDKYRP CSLGRLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT    50
    RIMCILRELY GVGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA 100
    GNSDRVVIQE MLKTVAQSQQ LETNSQRDFK VVLLTEVDKL TKDAQHALRR 150
    TMEKYMSTCR LILCCNSTSK VIPPIRSRCL AVRVPAPSIE DICHVLSTVC 200
    KKEGLNLPSQ LAHRLAEKSC RNLRKALLMC EACRVQQYPF TADQEIPETD 250
    WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL 300
    HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG 350
    LEGMMF 356
    Length:356
    Mass (Da):40,556
    Last modified:December 15, 1998 - v2
    Checksum:i820C11675A2C63A5
    GO
    Isoform 2 (identifier: P40938-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         294-356: GLLSELLHNCDGQLKGEVAQMAAYYEHRLQLGSKAIYHLEAFVAKFMALYKKFMEDGLEGMMF → ACKEESRSCDIF

    Note: No experimental confirmation available.

    Show »
    Length:305
    Mass (Da):34,756
    Checksum:i2835F2D0A4DDF1E4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161L → V.1 Publication
    Corresponds to variant rs3135533 [ dbSNP | Ensembl ].
    VAR_018750

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei294 – 35663GLLSE…EGMMF → ACKEESRSCDIF in isoform 2. 1 PublicationVSP_044920Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07541 mRNA. Translation: AAB07268.1.
    AF484446 Genomic DNA. Translation: AAL82505.1.
    AL139081 Genomic DNA. Translation: CAH70947.1.
    AL160394 Genomic DNA. No translation available.
    AL161891 Genomic DNA. No translation available.
    CH471075 Genomic DNA. Translation: EAX08537.1.
    BC000149 mRNA. Translation: AAH00149.1.
    CX786577 mRNA. No translation available.
    CCDSiCCDS45025.1. [P40938-2]
    CCDS9352.1. [P40938-1]
    PIRiT09573.
    RefSeqiNP_002906.1. NM_002915.3. [P40938-1]
    NP_853536.2. NM_181558.2. [P40938-2]
    UniGeneiHs.115474.

    Genome annotation databases

    EnsembliENST00000380071; ENSP00000369411; ENSG00000133119. [P40938-1]
    ENST00000434425; ENSP00000401001; ENSG00000133119. [P40938-2]
    GeneIDi5983.
    KEGGihsa:5983.
    UCSCiuc001uuz.3. human. [P40938-1]

    Polymorphism databases

    DMDMi3915601.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07541 mRNA. Translation: AAB07268.1 .
    AF484446 Genomic DNA. Translation: AAL82505.1 .
    AL139081 Genomic DNA. Translation: CAH70947.1 .
    AL160394 Genomic DNA. No translation available.
    AL161891 Genomic DNA. No translation available.
    CH471075 Genomic DNA. Translation: EAX08537.1 .
    BC000149 mRNA. Translation: AAH00149.1 .
    CX786577 mRNA. No translation available.
    CCDSi CCDS45025.1. [P40938-2 ]
    CCDS9352.1. [P40938-1 ]
    PIRi T09573.
    RefSeqi NP_002906.1. NM_002915.3. [P40938-1 ]
    NP_853536.2. NM_181558.2. [P40938-2 ]
    UniGenei Hs.115474.

    3D structure databases

    ProteinModelPortali P40938.
    SMRi P40938. Positions 4-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111915. 29 interactions.
    DIPi DIP-36432N.
    IntActi P40938. 13 interactions.
    MINTi MINT-3015032.
    STRINGi 9606.ENSP00000369411.

    PTM databases

    PhosphoSitei P40938.

    Polymorphism databases

    DMDMi 3915601.

    Proteomic databases

    MaxQBi P40938.
    PaxDbi P40938.
    PeptideAtlasi P40938.
    PRIDEi P40938.

    Protocols and materials databases

    DNASUi 5983.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380071 ; ENSP00000369411 ; ENSG00000133119 . [P40938-1 ]
    ENST00000434425 ; ENSP00000401001 ; ENSG00000133119 . [P40938-2 ]
    GeneIDi 5983.
    KEGGi hsa:5983.
    UCSCi uc001uuz.3. human. [P40938-1 ]

    Organism-specific databases

    CTDi 5983.
    GeneCardsi GC13P034392.
    HGNCi HGNC:9971. RFC3.
    HPAi HPA030149.
    MIMi 600405. gene.
    neXtProti NX_P40938.
    PharmGKBi PA34340.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0470.
    HOGENOMi HOG000224153.
    HOVERGENi HBG040509.
    InParanoidi P40938.
    KOi K10756.
    OMAi TRIMCLL.
    OrthoDBi EOG7FXZZD.
    PhylomeDBi P40938.
    TreeFami TF105724.

    Enzyme and pathway databases

    Reactomei REACT_1792. Polymerase switching.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_7987. Polymerase switching on the C-strand of the telomere.

    Miscellaneous databases

    ChiTaRSi RFC3. human.
    GeneWikii RFC3.
    GenomeRNAii 5983.
    NextBioi 23291.
    PROi P40938.
    SOURCEi Search...

    Gene expression databases

    Bgeei P40938.
    CleanExi HS_RFC3.
    Genevestigatori P40938.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR008921. DNA_pol3_clamp-load_cplx_C.
    IPR027417. P-loop_NTPase.
    IPR013748. Rep_factorC_C_dom.
    [Graphical view ]
    Pfami PF08542. Rep_fac_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48019. SSF48019. 1 hit.
    SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Homology in accessory proteins of replicative polymerases -- E. coli to humans."
      O'Donnell M., Onrust R., Dean F.B., Chen M., Hurwitz J.
      Nucleic Acids Res. 21:1-3(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. NIEHS SNPs program
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-16.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-305 (ISOFORM 2).
      Tissue: Embryonic stem cell and Placenta.
    6. "The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9."
      Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.
      J. Biol. Chem. 275:29767-29771(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD17.
    7. "Purification and characterization of human DNA damage checkpoint Rad complexes."
      Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD17.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "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-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRFC3_HUMAN
    AccessioniPrimary (citable) accession number: P40938
    Secondary accession number(s): C9JU95, O15252, Q5W0E8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3