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P35250

- RFC2_HUMAN

UniProt

P35250 - RFC2_HUMAN

Protein

Replication factor C subunit 2

Gene

RFC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      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. This subunit binds ATP By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi76 – 838ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: ProtInc
    2. DNA binding Source: InterPro
    3. nucleoside-triphosphatase activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. DNA replication Source: Reactome
    3. DNA strand elongation involved in DNA replication Source: Reactome
    4. mitotic cell cycle Source: Reactome
    5. nucleotide-excision repair Source: Reactome
    6. nucleotide-excision repair, DNA gap filling Source: Reactome
    7. telomere maintenance Source: Reactome
    8. telomere maintenance via recombination Source: Reactome
    9. telomere maintenance via semi-conservative replication Source: Reactome
    10. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-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 2
    Alternative name(s):
    Activator 1 40 kDa subunit
    Short name:
    A1 40 kDa subunit
    Activator 1 subunit 2
    Replication factor C 40 kDa subunit
    Short name:
    RF-C 40 kDa subunit
    Short name:
    RFC40
    Gene namesi
    Name:RFC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9970. RFC2.

    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

    Involvement in diseasei

    RFC2 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.

    Keywords - Diseasei

    Williams-Beuren syndrome

    Organism-specific databases

    MIMi194050. phenotype.
    Orphaneti904. Williams syndrome.
    PharmGKBiPA34339.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Replication factor C subunit 2PRO_0000121766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei163 – 1631N6-acetyllysine1 Publication
    Modified residuei304 – 3041N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP35250.
    PaxDbiP35250.
    PeptideAtlasiP35250.
    PRIDEiP35250.

    PTM databases

    PhosphoSiteiP35250.

    Expressioni

    Gene expression databases

    ArrayExpressiP35250.
    BgeeiP35250.
    CleanExiHS_RFC2.
    GenevestigatoriP35250.

    Organism-specific databases

    HPAiHPA029493.

    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. RFC2 also interacts with PRKAR1A; the complex may be involved in cell survival.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKAR1AP106447EBI-476409,EBI-476431
    RFC1P352514EBI-476409,EBI-476616
    RFC4P352498EBI-476409,EBI-476655

    Protein-protein interaction databases

    BioGridi111914. 43 interactions.
    DIPiDIP-34367N.
    IntActiP35250. 13 interactions.
    MINTiMINT-3013724.
    STRINGi9606.ENSP00000055077.

    Structurei

    3D structure databases

    ProteinModelPortaliP35250.
    SMRiP35250. Positions 35-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the activator 1 small subunits family.Curated

    Phylogenomic databases

    eggNOGiCOG0470.
    HOGENOMiHOG000224155.
    HOVERGENiHBG002053.
    InParanoidiP35250.
    KOiK10755.
    OMAiYSGTTRF.
    PhylomeDBiP35250.
    TreeFamiTF300585.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR008921. DNA_pol3_clamp-load_cplx_C.
    IPR027417. P-loop_NTPase.
    IPR013748. Rep_factorC_C_dom.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF08542. 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: P35250-1) [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

    MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI    50
    VGNEDTVSRL EVFAREGNVP NIIIAGPPGT GKTTSILCLA RALLGPALKD 100
    AMLELNASND RGIDVVRNKI KMFAQQKVTL PKGRHKIIIL DEADSMTDGA 150
    QQALRRTMEI YSKTTRFALA CNASDKIIEP IQSRCAVLRY TKLTDAQILT 200
    RLMNVIEKER VPYTDDGLEA IIFTAQGDMR QALNNLQSTF SGFGFINSEN 250
    VFKVCDEPHP LLVKEMIQHC VNANIDEAYK ILAHLWHLGY SPEDIIGNIF 300
    RVCKTFQMAE YLKLEFIKEI GYTHMKIAEG VNSLLQMAGL LARLCQKTMA 350
    PVAS 354
    Length:354
    Mass (Da):39,157
    Last modified:November 1, 1997 - v3
    Checksum:iB50AC8EEF89F64A9
    GO
    Isoform 2 (identifier: P35250-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-144: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:320
    Mass (Da):35,244
    Checksum:iD6E72DD28EA014E8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441G → L AA sequence (PubMed:1313560)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti232 – 2321A → V.1 Publication
    Corresponds to variant rs3135684 [ dbSNP | Ensembl ].
    VAR_023126

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 14434Missing in isoform 2. 1 PublicationVSP_005660Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87338 mRNA. Translation: AAB09786.1.
    AF045555 Genomic DNA. Translation: AAC04860.1.
    AF483622 Genomic DNA. Translation: AAL82503.1.
    AC005081 Genomic DNA. Translation: AAP22334.1.
    AB451243 mRNA. Translation: BAG70057.1.
    CH471200 Genomic DNA. Translation: EAW69607.1.
    CH471200 Genomic DNA. Translation: EAW69608.1.
    BC002813 mRNA. Translation: AAH02813.1.
    CCDSiCCDS5567.1. [P35250-2]
    CCDS5568.1. [P35250-1]
    PIRiA42700.
    RefSeqiNP_001265720.1. NM_001278791.1.
    NP_001265721.1. NM_001278792.1.
    NP_001265722.1. NM_001278793.1.
    NP_002905.2. NM_002914.4. [P35250-2]
    NP_852136.1. NM_181471.2. [P35250-1]
    UniGeneiHs.647062.

    Genome annotation databases

    EnsembliENST00000055077; ENSP00000055077; ENSG00000049541. [P35250-1]
    ENST00000352131; ENSP00000275627; ENSG00000049541. [P35250-2]
    GeneIDi5982.
    KEGGihsa:5982.
    UCSCiuc003uaj.3. human. [P35250-1]

    Polymorphism databases

    DMDMi2507300.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87338 mRNA. Translation: AAB09786.1 .
    AF045555 Genomic DNA. Translation: AAC04860.1 .
    AF483622 Genomic DNA. Translation: AAL82503.1 .
    AC005081 Genomic DNA. Translation: AAP22334.1 .
    AB451243 mRNA. Translation: BAG70057.1 .
    CH471200 Genomic DNA. Translation: EAW69607.1 .
    CH471200 Genomic DNA. Translation: EAW69608.1 .
    BC002813 mRNA. Translation: AAH02813.1 .
    CCDSi CCDS5567.1. [P35250-2 ]
    CCDS5568.1. [P35250-1 ]
    PIRi A42700.
    RefSeqi NP_001265720.1. NM_001278791.1.
    NP_001265721.1. NM_001278792.1.
    NP_001265722.1. NM_001278793.1.
    NP_002905.2. NM_002914.4. [P35250-2 ]
    NP_852136.1. NM_181471.2. [P35250-1 ]
    UniGenei Hs.647062.

    3D structure databases

    ProteinModelPortali P35250.
    SMRi P35250. Positions 35-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111914. 43 interactions.
    DIPi DIP-34367N.
    IntActi P35250. 13 interactions.
    MINTi MINT-3013724.
    STRINGi 9606.ENSP00000055077.

    PTM databases

    PhosphoSitei P35250.

    Polymorphism databases

    DMDMi 2507300.

    Proteomic databases

    MaxQBi P35250.
    PaxDbi P35250.
    PeptideAtlasi P35250.
    PRIDEi P35250.

    Protocols and materials databases

    DNASUi 5982.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000055077 ; ENSP00000055077 ; ENSG00000049541 . [P35250-1 ]
    ENST00000352131 ; ENSP00000275627 ; ENSG00000049541 . [P35250-2 ]
    GeneIDi 5982.
    KEGGi hsa:5982.
    UCSCi uc003uaj.3. human. [P35250-1 ]

    Organism-specific databases

    CTDi 5982.
    GeneCardsi GC07M073645.
    HGNCi HGNC:9970. RFC2.
    HPAi HPA029493.
    MIMi 194050. phenotype.
    600404. gene.
    neXtProti NX_P35250.
    Orphaneti 904. Williams syndrome.
    PharmGKBi PA34339.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0470.
    HOGENOMi HOG000224155.
    HOVERGENi HBG002053.
    InParanoidi P35250.
    KOi K10755.
    OMAi YSGTTRF.
    PhylomeDBi P35250.
    TreeFami TF300585.

    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 RFC2. human.
    GeneWikii RFC2.
    GenomeRNAii 5982.
    NextBioi 23285.
    PROi P35250.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35250.
    Bgeei P35250.
    CleanExi HS_RFC2.
    Genevestigatori P35250.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR008921. DNA_pol3_clamp-load_cplx_C.
    IPR027417. P-loop_NTPase.
    IPR013748. Rep_factorC_C_dom.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    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. "Sequence and expression in Escherichia coli of the 40-kDa subunit of activator 1 (replication factor C) of HeLa cells."
      Chen M., Pan Z.-Q., Hurwitz J.
      Proc. Natl. Acad. Sci. U.S.A. 89:2516-2520(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 232-249.
    2. Hurwitz J.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23."
      Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V., Koop B.F.
      Mamm. Genome 11:890-898(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    4. NIEHS SNPs program
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-232.
    5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 2).
      Tissue: Placenta.
    9. "The second subunit of the replication factor C complex (RFC40) and the regulatory subunit (RIalpha) of protein kinase A form a protein complex promoting cell survival."
      Gupte R.S., Weng Y., Liu L., Lee M.Y.
      Cell Cycle 4:323-329(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKAR1A.
    10. "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 AND LYS-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRFC2_HUMAN
    AccessioniPrimary (citable) accession number: P35250
    Secondary accession number(s): B5BU07
    , D3DXG3, P32846, Q9BU93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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