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P35251

- RFC1_HUMAN

UniProt

P35251 - RFC1_HUMAN

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Protein

Replication factor C subunit 1

Gene
RFC1, RFC140
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 6578ATP Reviewed prediction

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
Complete GO annotation...

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
Complete GO annotation...

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. 11 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.

Miscellaneous databases

EvolutionaryTraceiP35251.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini402 – 49291BRCTAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1120 – 11245Nuclear localization signal Reviewed prediction

Sequence similaritiesi

Contains 1 BRCT domain.

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

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. VSP_008443

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261E → K in AAA16121. 1 Publication
Sequence conflicti567 – 5671S → N in AAH51786. 1 Publication
Sequence conflicti629 – 6291A → S1 Publication
Sequence conflicti629 – 6291A → S1 Publication
Sequence conflicti629 – 6291A → S1 Publication
Sequence conflicti641 – 6411G → N1 Publication
Sequence conflicti641 – 6411G → N1 Publication
Sequence conflicti641 – 6411G → N1 Publication
Sequence conflicti677 – 6771A → R1 Publication
Sequence conflicti677 – 6771A → R1 Publication
Sequence conflicti677 – 6771A → R1 Publication
Sequence conflicti1076 – 10761S → A1 Publication
Sequence conflicti1076 – 10761S → A1 Publication
Sequence conflicti1076 – 10761S → A1 Publication

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. 11 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 159 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

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