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P35251 (RFC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RFC1
Synonyms:RFC140
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1148 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

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. Ref.9

Subunit structure

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. Ref.9

Subcellular location

Nucleus.

Tissue specificity

Wide tissue distribution. Undetectable in placental tissue.

Sequence similarities

Belongs to the activator 1 large subunit family.

Contains 1 BRCT domain.

Ontologies

Keywords
   Biological processDNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

DNA-dependent DNA replication

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Traceable author statement PubMed 8954124. Source: GOC

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

telomere maintenance via telomerase

Traceable author statement PubMed 8954124. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentDNA replication factor C complex

Inferred from direct assay PubMed 9488738. Source: UniProtKB

Golgi apparatus

Inferred from direct assay. Source: HPA

cell junction

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

DNA clamp loader activity

Inferred from electronic annotation. Source: InterPro

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

enzyme activator activity

Traceable author statement PubMed 8954124. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 16438930. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RFC2P352504EBI-476616,EBI-476409

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35251-1)

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.
Isoform 2 (identifier: P35251-2)

The sequence of this isoform differs from the canonical sequence as follows:
     630-630: Missing.
Note: Alternative use of an acceptor site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11481148Replication factor C subunit 1
PRO_0000121772

Regions

Domain402 – 49291BRCT
Nucleotide binding650 – 6578ATP Potential
Motif1120 – 11245Nuclear localization signal Potential

Amino acid modifications

Modified residue671Phosphotyrosine Ref.17 Ref.19
Modified residue691Phosphoserine Ref.12 Ref.14 Ref.16 Ref.17 Ref.19
Modified residue711Phosphoserine Ref.12 Ref.14 Ref.16 Ref.17 Ref.19
Modified residue731Phosphoserine Ref.14
Modified residue1081Phosphoserine Ref.14 Ref.17
Modified residue1101Phosphothreonine Ref.14 Ref.17
Modified residue1561Phosphoserine Ref.14 Ref.16 Ref.17
Modified residue1611Phosphothreonine Ref.14 Ref.16
Modified residue1631Phosphothreonine Ref.16
Modified residue1641Phosphoserine Ref.14 Ref.16
Modified residue1731Phosphoserine Ref.14 Ref.16 Ref.17
Modified residue1901Phosphoserine Ref.13 Ref.14 Ref.17 Ref.19
Modified residue2811Phosphoserine Ref.14
Modified residue2831Phosphoserine Ref.14
Modified residue3121Phosphoserine Ref.14 Ref.17
Modified residue3681Phosphoserine Ref.17 Ref.19
Modified residue11041Phosphoserine Ref.14
Modified residue11061Phosphoserine Ref.14

Natural variations

Alternative sequence6301Missing in isoform 2.
VSP_008443
Natural variant5981I → V. Ref.5
Corresponds to variant rs2066791 [ dbSNP | Ensembl ].
VAR_014860
Natural variant6131R → L. Ref.2 Ref.3 Ref.4
Corresponds to variant rs1057747 [ dbSNP | Ensembl ].
VAR_016986
Natural variant6921E → D. Ref.5
Corresponds to variant rs11932767 [ dbSNP | Ensembl ].
VAR_020657
Natural variant9551Q → K. Ref.5
Corresponds to variant rs17335452 [ dbSNP | Ensembl ].
VAR_020658
Natural variant11461S → L. Ref.5
Corresponds to variant rs17288828 [ dbSNP | Ensembl ].
VAR_020659

Experimental info

Sequence conflict3261E → K in AAA16121. Ref.1
Sequence conflict5671S → N in AAH51786. Ref.8
Sequence conflict6291A → S Ref.2
Sequence conflict6291A → S Ref.3
Sequence conflict6291A → S Ref.4
Sequence conflict6411G → N Ref.2
Sequence conflict6411G → N Ref.3
Sequence conflict6411G → N Ref.4
Sequence conflict6771A → R Ref.2
Sequence conflict6771A → R Ref.3
Sequence conflict6771A → R Ref.4
Sequence conflict10761S → A Ref.2
Sequence conflict10761S → A Ref.3
Sequence conflict10761S → A Ref.4

Secondary structure

...................... 1148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 4.
Checksum: 485F0332FB56819B

FASTA1,148128,255
        10         20         30         40         50         60 
MDIRKFFGVI PSGKKLVSET VKKNEKTKSD EETLKAKKGI KEIKVNSSRK EDDFKQKQPS 

        70         80         90        100        110        120 
KKKRIIYDSD SESEETLQVK NAKKPPEKLP VSSKPGKISR QDPVTYISET DEEDDFMCKK 

       130        140        150        160        170        180 
AASKSKENGR STNSHLGTSN MKKNEENTKT KNKPLSPIKL TPTSVLDYFG TGSVQRSNKK 

       190        200        210        220        230        240 
MVASKRKELS QNTDESGLND EAIAKQLQLD EDAELERQLH EDEEFARTLA MLDEEPKTKK 

       250        260        270        280        290        300 
ARKDTEAGET FSSVQANLSK AEKHKYPHKV KTAQVSDERK SYSPRKQSKY ESSKESQQHS 

       310        320        330        340        350        360 
KSSADKIGEV SSPKASSKLA IMKRKEESSY KEIEPVASKR KENAIKLKGE TKTPKKTKSS 

       370        380        390        400        410        420 
PAKKESVSPE DSEKKRTNYQ AYRSYLNREG PKALGSKEIP KGAENCLEGL IFVITGVLES 

       430        440        450        460        470        480 
IERDEAKSLI ERYGGKVTGN VSKKTNYLVM GRDSGQSKSD KAAALGTKII DEDGLLNLIR 

       490        500        510        520        530        540 
TMPGKKSKYE IAVETEMKKE SKLERTPQKN VQGKRKISPS KKESESKKSR PTSKRDSLAK 

       550        560        570        580        590        600 
TIKKETDVFW KSLDFKEQVA EETSGDSKAR NLADDSSENK VENLLWVDKY KPTSLKTIIG 

       610        620        630        640        650        660 
QQGDQSCANK LLRWLRNWQK SSSEDKKHAA KFGKFSGKDD GSSFKAALLS GPPGVGKTTT 

       670        680        690        700        710        720 
ASLVCQELGY SYVELNASDT RSKSSLKAIV AESLNNTSIK GFYSNGAASS VSTKHALIMD 

       730        740        750        760        770        780 
EVDGMAGNED RGGIQELIGL IKHTKIPIIC MCNDRNHPKI RSLVHYCFDL RFQRPRVEQI 

       790        800        810        820        830        840 
KGAMMSIAFK EGLKIPPPAM NEIILGANQD IRQVLHNLSM WCARSKALTY DQAKADSHRA 

       850        860        870        880        890        900 
KKDIKMGPFD VARKVFAAGE ETAHMSLVDK SDLFFHDYSI APLFVQENYI HVKPVAAGGD 

       910        920        930        940        950        960 
MKKHLMLLSR AADSICDGDL VDSQIRSKQN WSLLPAQAIY ASVLPGELMR GYMTQFPTFP 

       970        980        990       1000       1010       1020 
SWLGKHSSTG KHDRIVQDLA LHMSLRTYSS KRTVNMDYLS LLRDALVQPL TSQGVDGVQD 

      1030       1040       1050       1060       1070       1080 
VVALMDTYYL MKEDFENIME ISSWGGKPSP FSKLDPKVKA AFTRAYNKEA HLTPYSLQAI 

      1090       1100       1110       1120       1130       1140 
KASRHSTSPS LDSEYNEELN EDDSQSDEKD QDAIETDAMI KKKTKSSKPS KPEKDKEPRK 


GKGKSSKK 

« Hide

Isoform 2 [UniParc].

Checksum: D40A9F6F5CEB61AF
Show »

FASTA1,147128,183

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3450.1. [P35251-2]
CCDS56329.1. [P35251-1]
PIRA49651.
JN0599.
RefSeqNP_001191676.1. NM_001204747.1. [P35251-1]
NP_002904.3. NM_002913.4. [P35251-2]
UniGeneHs.507475.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBUNMR-A392-496[»]
2K6GNMR-A375-480[»]
2K7FNMR-A375-480[»]
ProteinModelPortalP35251.
SMRP35251. Positions 392-496, 583-818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111913. 46 interactions.
IntActP35251. 11 interactions.
MINTMINT-131797.
STRING9606.ENSP00000261424.

PTM databases

PhosphoSiteP35251.

Polymorphism databases

DMDM56757608.

Proteomic databases

MaxQBP35251.
PaxDbP35251.
PRIDEP35251.

Protocols and materials databases

DNASU5981.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349703; ENSP00000261424; ENSG00000035928. [P35251-2]
ENST00000381897; ENSP00000371321; ENSG00000035928. [P35251-1]
GeneID5981.
KEGGhsa:5981.
UCSCuc003gtx.2. human. [P35251-2]
uc003gty.2. human. [P35251-1]

Organism-specific databases

CTD5981.
GeneCardsGC04M039291.
HGNCHGNC:9969. RFC1.
HPACAB009520.
HPA046116.
HPA058107.
MIM102579. gene.
neXtProtNX_P35251.
PharmGKBPA34338.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5275.
HOGENOMHOG000013116.
HOVERGENHBG004167.
InParanoidP35251.
KOK10754.
OMAWAKNDDG.
OrthoDBEOG7N63M2.
PhylomeDBP35251.
TreeFamTF105722.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.
SignaLinkP35251.

Gene expression databases

ArrayExpressP35251.
BgeeP35251.
CleanExHS_RFC1.
GenevestigatorP35251.

Family and domain databases

Gene3D3.40.50.10190. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003593. 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]
PfamPF00004. AAA. 1 hit.
PF00533. BRCT. 1 hit.
PF08519. RFC1. 1 hit.
[Graphical view]
PIRSFPIRSF036578. RFC1. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF48019. SSF48019. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
[Graphical view]
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Other

ChiTaRSRFC1. human.
EvolutionaryTraceP35251.
GeneWikiRFC1.
GenomeRNAi5981.
NextBio23281.
PMAP-CutDBP35251.
PROP35251.
SOURCESearch...

Entry information

Entry nameRFC1_HUMAN
AccessionPrimary (citable) accession number: P35251
Secondary accession number(s): A8K6E7 expand/collapse secondary AC list , Q5XKF5, Q6PKU0, Q86V41, Q86V46
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM