Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P35251

- RFC1_HUMAN

UniProt

P35251 - RFC1_HUMAN

Protein

Replication factor C subunit 1

Gene

RFC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.1 Publication
    Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi650 – 6578ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: ProtInc
    2. DNA binding Source: RefGenome
    3. DNA clamp loader activity Source: InterPro
    4. double-stranded DNA binding Source: Ensembl
    5. enzyme activator activity Source: ProtInc
    6. protein binding Source: UniProtKB
    7. sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. DNA-dependent DNA replication Source: ProtInc
    2. DNA repair Source: Reactome
    3. DNA strand elongation involved in DNA replication Source: Reactome
    4. mitotic cell cycle Source: Reactome
    5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. nucleotide-excision repair Source: Reactome
    7. nucleotide-excision repair, DNA gap filling Source: Reactome
    8. positive regulation of catalytic activity Source: GOC
    9. positive regulation of transcription, DNA-templated Source: Ensembl
    10. telomere maintenance Source: Reactome
    11. telomere maintenance via recombination Source: Reactome
    12. telomere maintenance via semi-conservative replication Source: Reactome
    13. telomere maintenance via telomerase Source: ProtInc
    14. transcription, DNA-templated Source: UniProtKB-KW
    15. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    DNA replication, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-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_7987. Polymerase switching on the C-strand of the telomere.
    SignaLinkiP35251.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replication factor C subunit 1
    Alternative name(s):
    Activator 1 140 kDa subunit
    Short name:
    A1 140 kDa subunit
    Activator 1 large subunit
    Activator 1 subunit 1
    DNA-binding protein PO-GA
    Replication factor C 140 kDa subunit
    Short name:
    RF-C 140 kDa subunit
    Short name:
    RFC140
    Replication factor C large subunit
    Gene namesi
    Name:RFC1
    Synonyms:RFC140
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9969. RFC1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. DNA replication factor C complex Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34338.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11481148Replication factor C subunit 1PRO_0000121772Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphotyrosine2 Publications
    Modified residuei69 – 691Phosphoserine5 Publications
    Modified residuei71 – 711Phosphoserine5 Publications
    Modified residuei73 – 731Phosphoserine1 Publication
    Modified residuei108 – 1081Phosphoserine2 Publications
    Modified residuei110 – 1101Phosphothreonine2 Publications
    Modified residuei156 – 1561Phosphoserine3 Publications
    Modified residuei161 – 1611Phosphothreonine2 Publications
    Modified residuei163 – 1631Phosphothreonine1 Publication
    Modified residuei164 – 1641Phosphoserine2 Publications
    Modified residuei173 – 1731Phosphoserine3 Publications
    Modified residuei190 – 1901Phosphoserine4 Publications
    Modified residuei281 – 2811Phosphoserine1 Publication
    Modified residuei283 – 2831Phosphoserine1 Publication
    Modified residuei312 – 3121Phosphoserine2 Publications
    Modified residuei368 – 3681Phosphoserine2 Publications
    Modified residuei1104 – 11041Phosphoserine1 Publication
    Modified residuei1106 – 11061Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP35251.
    PaxDbiP35251.
    PRIDEiP35251.

    PTM databases

    PhosphoSiteiP35251.

    Miscellaneous databases

    PMAP-CutDBP35251.

    Expressioni

    Tissue specificityi

    Wide tissue distribution. Undetectable in placental tissue.

    Gene expression databases

    ArrayExpressiP35251.
    BgeeiP35251.
    CleanExiHS_RFC1.
    GenevestigatoriP35251.

    Organism-specific databases

    HPAiCAB009520.
    HPA046116.
    HPA058107.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RFC2P352504EBI-476616,EBI-476409

    Protein-protein interaction databases

    BioGridi111913. 46 interactions.
    IntActiP35251. 12 interactions.
    MINTiMINT-131797.
    STRINGi9606.ENSP00000261424.

    Structurei

    Secondary structure

    1
    1148
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi380 – 3867
    Turni394 – 3963
    Beta strandi404 – 4074
    Beta strandi411 – 4144
    Beta strandi419 – 4213
    Helixi423 – 43210
    Beta strandi436 – 4405
    Beta strandi447 – 4504
    Helixi457 – 4659
    Beta strandi468 – 4714
    Helixi472 – 48110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EBUNMR-A392-496[»]
    2K6GNMR-A375-480[»]
    2K7FNMR-A375-480[»]
    ProteinModelPortaliP35251.
    SMRiP35251. Positions 392-496, 583-818.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35251.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini402 – 49291BRCTPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1120 – 11245Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the activator 1 large subunit family.Curated
    Contains 1 BRCT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5275.
    HOGENOMiHOG000013116.
    HOVERGENiHBG004167.
    InParanoidiP35251.
    KOiK10754.
    OMAiWAKNDDG.
    OrthoDBiEOG7N63M2.
    PhylomeDBiP35251.
    TreeFamiTF105722.

    Family and domain databases

    Gene3Di3.40.50.10190. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR001357. BRCT_dom.
    IPR008921. DNA_pol3_clamp-load_cplx_C.
    IPR012178. DNA_replication_fac_C_lsu.
    IPR013725. DNA_replication_fac_RFC1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF00533. BRCT. 1 hit.
    PF08519. RFC1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036578. RFC1. 1 hit.
    SMARTiSM00382. AAA. 1 hit.
    SM00292. BRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF48019. SSF48019. 1 hit.
    SSF52113. SSF52113. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35251-1) [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

    MDIRKFFGVI PSGKKLVSET VKKNEKTKSD EETLKAKKGI KEIKVNSSRK     50
    EDDFKQKQPS KKKRIIYDSD SESEETLQVK NAKKPPEKLP VSSKPGKISR 100
    QDPVTYISET DEEDDFMCKK AASKSKENGR STNSHLGTSN MKKNEENTKT 150
    KNKPLSPIKL TPTSVLDYFG TGSVQRSNKK MVASKRKELS QNTDESGLND 200
    EAIAKQLQLD EDAELERQLH EDEEFARTLA MLDEEPKTKK ARKDTEAGET 250
    FSSVQANLSK AEKHKYPHKV KTAQVSDERK SYSPRKQSKY ESSKESQQHS 300
    KSSADKIGEV SSPKASSKLA IMKRKEESSY KEIEPVASKR KENAIKLKGE 350
    TKTPKKTKSS PAKKESVSPE DSEKKRTNYQ AYRSYLNREG PKALGSKEIP 400
    KGAENCLEGL IFVITGVLES IERDEAKSLI ERYGGKVTGN VSKKTNYLVM 450
    GRDSGQSKSD KAAALGTKII DEDGLLNLIR TMPGKKSKYE IAVETEMKKE 500
    SKLERTPQKN VQGKRKISPS KKESESKKSR PTSKRDSLAK TIKKETDVFW 550
    KSLDFKEQVA EETSGDSKAR NLADDSSENK VENLLWVDKY KPTSLKTIIG 600
    QQGDQSCANK LLRWLRNWQK SSSEDKKHAA KFGKFSGKDD GSSFKAALLS 650
    GPPGVGKTTT ASLVCQELGY SYVELNASDT RSKSSLKAIV AESLNNTSIK 700
    GFYSNGAASS VSTKHALIMD EVDGMAGNED RGGIQELIGL IKHTKIPIIC 750
    MCNDRNHPKI RSLVHYCFDL RFQRPRVEQI KGAMMSIAFK EGLKIPPPAM 800
    NEIILGANQD IRQVLHNLSM WCARSKALTY DQAKADSHRA KKDIKMGPFD 850
    VARKVFAAGE ETAHMSLVDK SDLFFHDYSI APLFVQENYI HVKPVAAGGD 900
    MKKHLMLLSR AADSICDGDL VDSQIRSKQN WSLLPAQAIY ASVLPGELMR 950
    GYMTQFPTFP SWLGKHSSTG KHDRIVQDLA LHMSLRTYSS KRTVNMDYLS 1000
    LLRDALVQPL TSQGVDGVQD VVALMDTYYL MKEDFENIME ISSWGGKPSP 1050
    FSKLDPKVKA AFTRAYNKEA HLTPYSLQAI KASRHSTSPS LDSEYNEELN 1100
    EDDSQSDEKD QDAIETDAMI KKKTKSSKPS KPEKDKEPRK GKGKSSKK 1148
    Length:1,148
    Mass (Da):128,255
    Last modified:December 21, 2004 - v4
    Checksum:i485F0332FB56819B
    GO
    Isoform 2 (identifier: P35251-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         630-630: Missing.

    Note: Alternative use of an acceptor site.

    Show »
    Length:1,147
    Mass (Da):128,183
    Checksum:iD40A9F6F5CEB61AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti326 – 3261E → K in AAA16121. (PubMed:8248204)Curated
    Sequence conflicti567 – 5671S → N in AAH51786. (PubMed:15489334)Curated
    Sequence conflicti629 – 6291A → S(PubMed:8512577)Curated
    Sequence conflicti629 – 6291A → S(PubMed:7914507)Curated
    Sequence conflicti629 – 6291A → S1 PublicationCurated
    Sequence conflicti641 – 6411G → N(PubMed:8512577)Curated
    Sequence conflicti641 – 6411G → N(PubMed:7914507)Curated
    Sequence conflicti641 – 6411G → N1 PublicationCurated
    Sequence conflicti677 – 6771A → R(PubMed:8512577)Curated
    Sequence conflicti677 – 6771A → R(PubMed:7914507)Curated
    Sequence conflicti677 – 6771A → R1 PublicationCurated
    Sequence conflicti1076 – 10761S → A(PubMed:8512577)Curated
    Sequence conflicti1076 – 10761S → A(PubMed:7914507)Curated
    Sequence conflicti1076 – 10761S → A1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti598 – 5981I → V.1 Publication
    Corresponds to variant rs2066791 [ dbSNP | Ensembl ].
    VAR_014860
    Natural varianti613 – 6131R → L.3 Publications
    Corresponds to variant rs1057747 [ dbSNP | Ensembl ].
    VAR_016986
    Natural varianti692 – 6921E → D.1 Publication
    Corresponds to variant rs11932767 [ dbSNP | Ensembl ].
    VAR_020657
    Natural varianti955 – 9551Q → K.1 Publication
    Corresponds to variant rs17335452 [ dbSNP | Ensembl ].
    VAR_020658
    Natural varianti1146 – 11461S → L.1 Publication
    Corresponds to variant rs17288828 [ dbSNP | Ensembl ].
    VAR_020659

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei630 – 6301Missing in isoform 2. 2 PublicationsVSP_008443

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23320 mRNA. Translation: AAA16121.1.
    Z22642 mRNA. Translation: CAA80355.1.
    AF040250 mRNA. Translation: AAB99788.1.
    AY600371 Genomic DNA. Translation: AAS94325.1.
    AK291612 mRNA. Translation: BAF84301.1.
    CH471069 Genomic DNA. Translation: EAW92923.1.
    BC035297 mRNA. Translation: AAH35297.1.
    BC051751 mRNA. Translation: AAH51751.1.
    BC051786 mRNA. Translation: AAH51786.1.
    CCDSiCCDS3450.1. [P35251-2]
    CCDS56329.1. [P35251-1]
    PIRiA49651.
    JN0599.
    RefSeqiNP_001191676.1. NM_001204747.1. [P35251-1]
    NP_002904.3. NM_002913.4. [P35251-2]
    UniGeneiHs.507475.

    Genome annotation databases

    EnsembliENST00000349703; ENSP00000261424; ENSG00000035928. [P35251-2]
    ENST00000381897; ENSP00000371321; ENSG00000035928. [P35251-1]
    GeneIDi5981.
    KEGGihsa:5981.
    UCSCiuc003gtx.2. human. [P35251-2]
    uc003gty.2. human. [P35251-1]

    Polymorphism databases

    DMDMi56757608.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23320 mRNA. Translation: AAA16121.1 .
    Z22642 mRNA. Translation: CAA80355.1 .
    AF040250 mRNA. Translation: AAB99788.1 .
    AY600371 Genomic DNA. Translation: AAS94325.1 .
    AK291612 mRNA. Translation: BAF84301.1 .
    CH471069 Genomic DNA. Translation: EAW92923.1 .
    BC035297 mRNA. Translation: AAH35297.1 .
    BC051751 mRNA. Translation: AAH51751.1 .
    BC051786 mRNA. Translation: AAH51786.1 .
    CCDSi CCDS3450.1. [P35251-2 ]
    CCDS56329.1. [P35251-1 ]
    PIRi A49651.
    JN0599.
    RefSeqi NP_001191676.1. NM_001204747.1. [P35251-1 ]
    NP_002904.3. NM_002913.4. [P35251-2 ]
    UniGenei Hs.507475.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EBU NMR - A 392-496 [» ]
    2K6G NMR - A 375-480 [» ]
    2K7F NMR - A 375-480 [» ]
    ProteinModelPortali P35251.
    SMRi P35251. Positions 392-496, 583-818.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111913. 46 interactions.
    IntActi P35251. 12 interactions.
    MINTi MINT-131797.
    STRINGi 9606.ENSP00000261424.

    PTM databases

    PhosphoSitei P35251.

    Polymorphism databases

    DMDMi 56757608.

    Proteomic databases

    MaxQBi P35251.
    PaxDbi P35251.
    PRIDEi P35251.

    Protocols and materials databases

    DNASUi 5981.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000349703 ; ENSP00000261424 ; ENSG00000035928 . [P35251-2 ]
    ENST00000381897 ; ENSP00000371321 ; ENSG00000035928 . [P35251-1 ]
    GeneIDi 5981.
    KEGGi hsa:5981.
    UCSCi uc003gtx.2. human. [P35251-2 ]
    uc003gty.2. human. [P35251-1 ]

    Organism-specific databases

    CTDi 5981.
    GeneCardsi GC04M039291.
    HGNCi HGNC:9969. RFC1.
    HPAi CAB009520.
    HPA046116.
    HPA058107.
    MIMi 102579. gene.
    neXtProti NX_P35251.
    PharmGKBi PA34338.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5275.
    HOGENOMi HOG000013116.
    HOVERGENi HBG004167.
    InParanoidi P35251.
    KOi K10754.
    OMAi WAKNDDG.
    OrthoDBi EOG7N63M2.
    PhylomeDBi P35251.
    TreeFami TF105722.

    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_7987. Polymerase switching on the C-strand of the telomere.
    SignaLinki P35251.

    Miscellaneous databases

    ChiTaRSi RFC1. human.
    EvolutionaryTracei P35251.
    GeneWikii RFC1.
    GenomeRNAii 5981.
    NextBioi 23281.
    PMAP-CutDB P35251.
    PROi P35251.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35251.
    Bgeei P35251.
    CleanExi HS_RFC1.
    Genevestigatori P35251.

    Family and domain databases

    Gene3Di 3.40.50.10190. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR001357. BRCT_dom.
    IPR008921. DNA_pol3_clamp-load_cplx_C.
    IPR012178. DNA_replication_fac_C_lsu.
    IPR013725. DNA_replication_fac_RFC1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF00533. BRCT. 1 hit.
    PF08519. RFC1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036578. RFC1. 1 hit.
    SMARTi SM00382. AAA. 1 hit.
    SM00292. BRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48019. SSF48019. 1 hit.
    SSF52113. SSF52113. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNAs encoding the large subunit of human replication factor C."
      Bunz F., Kobayashi R., Stillman B.
      Proc. Natl. Acad. Sci. U.S.A. 90:11014-11018(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 469-480; 571-580 AND 678-700.
    2. "Cloning and expression of a novel human DNA binding protein, PO-GA."
      Lu Y., Zeft A.S., Riegel A.T.
      Biochem. Biophys. Res. Commun. 193:779-786(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-613.
    3. "The human DNA-binding protein, PO-GA, is homologous to the large subunit of mouse replication factor C: regulation by alternate 3' processing of mRNA."
      Lu Y., Riegel A.T.
      Gene 145:261-265(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2), VARIANT LEU-613.
    4. "Molecular cloning of a DNA binding protein from human hepatoma cells."
      Rajavashisth T.B., Tripathi S.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2), VARIANT LEU-613.
      Tissue: Hepatoma.
    5. NIEHS SNPs program
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-598; ASP-692; LYS-955 AND LEU-1146.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    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] (ISOFORMS 1 AND 2).
      Tissue: Skin, Testis and Uterus.
    9. "Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen."
      Mossi R., Jonsson Z.O., Allen B.L., Hardin S.H., Huebscher U.
      J. Biol. Chem. 272:1769-1776(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PCNA.
    10. "DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C."
      Allen B.L., Uhlmann F., Gaur L.K., Mulder B.A., Posey K.L., Jones L.B., Hardin S.H.
      Nucleic Acids Res. 26:3877-3882(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-73; SER-108; THR-110; SER-156; THR-161; SER-164; SER-173; SER-190; SER-281; SER-283; SER-312; SER-1104 AND SER-1106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-156; THR-161; THR-163; SER-164 AND SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-69; SER-71; SER-108; THR-110; SER-156; SER-173; SER-190; SER-312 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-69; SER-71; SER-190 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Solution structure of the BRCT domain from human replication factor C large subunit 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 392-496.

    Entry informationi

    Entry nameiRFC1_HUMAN
    AccessioniPrimary (citable) accession number: P35251
    Secondary accession number(s): A8K6E7
    , Q5XKF5, Q6PKU0, Q86V41, Q86V46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 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

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

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3