Reviewed,
UniProtKB/Swiss-Prot P35251 (RFC1_HUMAN)
Last modified
November 24, 2009.
Version 112.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Replication factor C subunit 1 Alternative name(s): Activator 1 subunit 1 Replication factor C large subunit RF-C 140 kDa subunit Activator 1 140 kDa subunit Short name=A1 140 kDa subunit Activator 1 large subunit DNA-binding protein PO-GA | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1148 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| Tissue specificity | Wide tissue distribution. Undetectable in placental tissue. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 |
| Sequence similarities | Belongs to the activator 1 large subunit family. Contains 1 BRCT domain. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| RFC2 | P35250 | 1 | EBI-476616,EBI-476409 | |
| SMC1A | Q14683 | 1 | EBI-476616,EBI-80690 |
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1148 | 1148 | Replication factor C subunit 1 | PRO_0000121772 | ||||||||||||||||||||
Regions | ||||||||||||||||||||||||
| Domain | 402 – 492 | 91 | BRCT | |||||||||||||||||||||
| Nucleotide binding | 650 – 657 | 8 | ATP Potential | |||||||||||||||||||||
| Motif | 1120 – 1124 | 5 | Nuclear localization signal Potential | |||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||
| Modified residue | 67 | 1 | Phosphotyrosine | |||||||||||||||||||||
| Modified residue | 69 | 1 | Phosphoserine Ref.11 Ref.14 Ref.17 | |||||||||||||||||||||
| Modified residue | 71 | 1 | Phosphoserine Ref.11 Ref.12 Ref.14 Ref.17 | |||||||||||||||||||||
| Modified residue | 73 | 1 | Phosphoserine Ref.12 Ref.14 Ref.17 | |||||||||||||||||||||
| Modified residue | 108 | 1 | Phosphoserine Ref.11 Ref.17 | |||||||||||||||||||||
| Modified residue | 110 | 1 | Phosphothreonine Ref.17 | |||||||||||||||||||||
| Modified residue | 156 | 1 | Phosphoserine Ref.12 Ref.17 | |||||||||||||||||||||
| Modified residue | 161 | 1 | Phosphothreonine Ref.15 Ref.17 | |||||||||||||||||||||
| Modified residue | 163 | 1 | Phosphothreonine | |||||||||||||||||||||
| Modified residue | 164 | 1 | Phosphoserine Ref.17 | |||||||||||||||||||||
| Modified residue | 171 | 1 | Phosphothreonine Ref.17 | |||||||||||||||||||||
| Modified residue | 173 | 1 | Phosphoserine Ref.15 Ref.17 | |||||||||||||||||||||
| Modified residue | 190 | 1 | Phosphoserine Ref.11 Ref.16 Ref.17 | |||||||||||||||||||||
| Modified residue | 281 | 1 | Phosphoserine Ref.17 | |||||||||||||||||||||
| Modified residue | 283 | 1 | Phosphoserine Ref.17 | |||||||||||||||||||||
| Modified residue | 312 | 1 | Phosphoserine Ref.17 | |||||||||||||||||||||
| Modified residue | 634 | 1 | N6-acetyllysine Ref.21 | |||||||||||||||||||||
| Modified residue | 670 | 1 | Phosphotyrosine Ref.13 | |||||||||||||||||||||
| Modified residue | 672 | 1 | Phosphotyrosine Ref.13 | |||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||
| Alternative sequence | 630 | 1 | Missing in isoform 2. | VSP_008443 | ||||||||||||||||||||
| Natural variant | 598 | 1 | I → V: dbSNP rs2066791. Ref.5 | VAR_014860 | ||||||||||||||||||||
| Natural variant | 613 | 1 | R → L: dbSNP rs1057747. Ref.2 Ref.3 Ref.4 | VAR_016986 | ||||||||||||||||||||
| Natural variant | 692 | 1 | E → D | VAR_020657 | ||||||||||||||||||||
| Natural variant | 955 | 1 | Q → K | VAR_020658 | ||||||||||||||||||||
| Natural variant | 1146 | 1 | S → L | VAR_020659 | ||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||
| Sequence conflict | 326 | 1 | E → K in AAA16121. Ref.1 | |||||||||||||||||||||
| Sequence conflict | 567 | 1 | S → N in AAH51786. Ref.8 | |||||||||||||||||||||
| Sequence conflict | 629 | 1 | A → S Ref.2 | |||||||||||||||||||||
| Sequence conflict | 629 | 1 | A → S Ref.3 | |||||||||||||||||||||
| Sequence conflict | 629 | 1 | A → S Ref.4 | |||||||||||||||||||||
| Sequence conflict | 641 | 1 | G → N Ref.2 | |||||||||||||||||||||
| Sequence conflict | 641 | 1 | G → N Ref.3 | |||||||||||||||||||||
| Sequence conflict | 641 | 1 | G → N Ref.4 | |||||||||||||||||||||
| Sequence conflict | 677 | 1 | A → R Ref.2 | |||||||||||||||||||||
| Sequence conflict | 677 | 1 | A → R Ref.3 | |||||||||||||||||||||
| Sequence conflict | 677 | 1 | A → R Ref.4 | |||||||||||||||||||||
| Sequence conflict | 1076 | 1 | S → A Ref.2 | |||||||||||||||||||||
| Sequence conflict | 1076 | 1 | S → A Ref.3 | |||||||||||||||||||||
| Sequence conflict | 1076 | 1 | S → A Ref.4 | |||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||
| Beta strand | 404 – 407 | 4 | ||||||||||||||||||||||
| Beta strand | 411 – 414 | 4 | ||||||||||||||||||||||
| Beta strand | 419 – 421 | 3 | ||||||||||||||||||||||
| Helix | 423 – 432 | 10 | ||||||||||||||||||||||
| Beta strand | 447 – 450 | 4 | ||||||||||||||||||||||
| Helix | 457 – 465 | 9 | ||||||||||||||||||||||
| Beta strand | 468 – 471 | 4 | ||||||||||||||||||||||
| Helix | 472 – 481 | 10 | ||||||||||||||||||||||
Sequences
| ||||||||||||||||||||||||
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: 8248204] [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: 8512577] [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: 7914507] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. 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: 15489334] [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: 8999859] [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: 9705493] [Abstract] Cited for: DNA-BINDING. |
| [11] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-108 AND SER-190, MASS SPECTROMETRY. Tissue: Epithelium. |
| [12] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73 AND SER-156, MASS SPECTROMETRY. Tissue: Epithelium. |
| [13] | "Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-670 AND TYR-672, MASS SPECTROMETRY. |
| [14] | "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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71 AND SER-73, MASS SPECTROMETRY. Tissue: Epithelium. |
| [15] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161 AND SER-173, MASS SPECTROMETRY. Tissue: Epithelium. |
| [16] | "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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY. |
| [17] | "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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-73; SER-108; THR-110; SER-156; THR-161; SER-164; THR-171; SER-173; SER-190; SER-281; SER-283 AND SER-312, MASS SPECTROMETRY. |
| [18] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [19] | "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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-69; SER-71; SER-73 AND SER-312, MASS SPECTROMETRY. |
| [20] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-156; THR-161; THR-163; SER-164 AND SER-173, MASS SPECTROMETRY. Tissue: T-cell. |
| [21] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-634, MASS SPECTROMETRY. |
| [22] | "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. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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. | |||||||||||||||||||||||||
| IPI | IPI00375358. IPI00375359. | ||||||||||||||||||||||||
| PIR | A49651. JN0599. | ||||||||||||||||||||||||
| RefSeq | NP_002904.3. | ||||||||||||||||||||||||
| UniGene | Hs.507475 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P35251. 7 interactions. | ||||||||||||||||||||||||
| STRING | P35251. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | P35251. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PRIDE | P35251. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000381897; ENSP00000371321; ENSG00000035928; Homo sapiens. [Genome view] | ||||||||||||||||||||||||
| GeneID | 5981. | ||||||||||||||||||||||||
| KEGG | hsa:5981. | ||||||||||||||||||||||||
| UCSC | uc003gtx.1. human. uc003gty.1. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 5981. | ||||||||||||||||||||||||
| GeneCards | GC04M038965. | ||||||||||||||||||||||||
| H-InvDB | HIX0024551. | ||||||||||||||||||||||||
| HGNC | HGNC:9969. RFC1. | ||||||||||||||||||||||||
| HPA | CAB009520. | ||||||||||||||||||||||||
| MIM | 102579. gene. | ||||||||||||||||||||||||
| PharmGKB | PA34338. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P35251. | ||||||||||||||||||||||||
| HOVERGEN | P35251. | ||||||||||||||||||||||||
| OMA | LSPIKLT | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | CATTLE:ENSBTAG00000014515-MON. | ||||||||||||||||||||||||
| Pathway_Interaction_DB | faspathway. FAS signaling pathway (CD95). | ||||||||||||||||||||||||
| Reactome | REACT_152. Cell Cycle, Mitotic. REACT_216. DNA Repair. REACT_383. DNA Replication. REACT_7970. Telomere Maintenance. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P35251. | ||||||||||||||||||||||||
| Bgee | P35251. | ||||||||||||||||||||||||
| CleanEx | HS_RFC1. | ||||||||||||||||||||||||
| Genevestigator | P35251. | ||||||||||||||||||||||||
| GermOnline | ENSG00000035928. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR001357. BRCT. IPR008921. DNA_pol3_clamp-load_cplx_C. IPR012178. DNA_replication_fac_C_lsu. IPR013725. DNA_replication_fac_RFC1_C. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF00004. AAA. 1 hit. PF00533. BRCT. 1 hit. PF08519. RFC1. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PIRSF | PIRSF036578. RFC1. 1 hit. | ||||||||||||||||||||||||
| SMART | SM00382. AAA. 1 hit. SM00292. BRCT. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS50172. BRCT. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| NextBio | 23281. | ||||||||||||||||||||||||
| PMAP-CutDB | P35251. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | RFC1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P35251 Secondary accession number(s): A8K6E7 Q86V46 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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
| Human chromosome 4 Human chromosome 4: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


