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P40937

- RFC5_HUMAN

UniProt

P40937 - RFC5_HUMAN

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Protein

Replication factor C subunit 5

Gene

RFC5

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 proliferating cell nuclear antigen (PCNA) and activator 1.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi60 – 678ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. enzyme binding Source: UniProtKB

GO - Biological processi

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

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1792. Polymerase switching.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_6769. Activation of ATR in response to replication stress.
REACT_7987. Polymerase switching on the C-strand of the telomere.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 5
Alternative name(s):
Activator 1 36 kDa subunit
Short name:
A1 36 kDa subunit
Activator 1 subunit 5
Replication factor C 36 kDa subunit
Short name:
RF-C 36 kDa subunit
Short name:
RFC36
Gene namesi
Name:RFC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9973. RFC5.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. DNA replication factor C complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34342.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Replication factor C subunit 5PRO_0000121751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP40937.
PaxDbiP40937.
PRIDEiP40937.

PTM databases

PhosphoSiteiP40937.

Expressioni

Gene expression databases

BgeeiP40937.
CleanExiHS_RFC5.
ExpressionAtlasiP40937. baseline and differential.
GenevestigatoriP40937.

Organism-specific databases

HPAiHPA041037.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RFC4P352496EBI-712376,EBI-476655

Protein-protein interaction databases

BioGridi111917. 39 interactions.
DIPiDIP-36433N.
IntActiP40937. 15 interactions.
MINTiMINT-1372754.
STRINGi9606.ENSP00000408295.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LFSmodel-A1-340[»]
ProteinModelPortaliP40937.
SMRiP40937. Positions 19-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiCOG0470.
GeneTreeiENSGT00550000075072.
HOGENOMiHOG000224152.
HOVERGENiHBG002053.
InParanoidiP40937.
KOiK10756.
OMAiCTGNPHP.
PhylomeDBiP40937.
TreeFamiTF300810.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C_dom.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P40937-1) [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

        10         20         30         40         50
METSALKQQE QPAATKIRNL PWVEKYRPQT LNDLISHQDI LSTIQKFINE
60 70 80 90 100
DRLPHLLLYG PPGTGKTSTI LACAKQLYKD KEFGSMVLEL NASDDRGIDI
110 120 130 140 150
IRGPILSFAS TRTIFKKGFK LVILDEADAM TQDAQNALRR VIEKFTENTR
160 170 180 190 200
FCLICNYLSK IIPALQSRCT RFRFGPLTPE LMVPRLEHVV EEEKVDISED
210 220 230 240 250
GMKALVTLSS GDMRRALNIL QSTNMAFGKV TEETVYTCTG HPLKSDIANI
260 270 280 290 300
LDWMLNQDFT TAYRNITELK TLKGLALHDI LTEIHLFVHR VDFPSSVRIH
310 320 330 340
LLTKMADIEY RLSVGTNEKI QLSSLIAAFQ VTRDLIVAEA
Length:340
Mass (Da):38,497
Last modified:February 1, 1995 - v1
Checksum:iE31E7B8C79933BCE
GO
Isoform 2 (identifier: P40937-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: METSALKQQEQPAATKIRNLPW → M

Note: No experimental confirmation available.

Show »
Length:319
Mass (Da):36,105
Checksum:i6F284482080E75DB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131A → T.1 Publication
Corresponds to variant rs5745796 [ dbSNP | Ensembl ].
VAR_018749

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222METSA…RNLPW → M in isoform 2. 1 PublicationVSP_043067Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07540 mRNA. Translation: AAB09784.1.
AY254323 Genomic DNA. Translation: AAO63493.1.
AK094575 mRNA. Translation: BAG52890.1.
AC131159 Genomic DNA. No translation available.
BC001866 mRNA. Translation: AAH01866.1.
BC013961 mRNA. Translation: AAH13961.1.
CCDSiCCDS41843.2. [P40937-2]
CCDS9185.1. [P40937-1]
RefSeqiNP_001123584.1. NM_001130112.2.
NP_031396.1. NM_007370.5. [P40937-1]
NP_853556.2. NM_181578.3. [P40937-2]
UniGeneiHs.731908.

Genome annotation databases

EnsembliENST00000392542; ENSP00000376325; ENSG00000111445. [P40937-2]
ENST00000454402; ENSP00000408295; ENSG00000111445. [P40937-1]
GeneIDi5985.
KEGGihsa:5985.
UCSCiuc001twq.3. human. [P40937-1]
uc010syx.2. human. [P40937-2]

Polymorphism databases

DMDMi728777.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07540 mRNA. Translation: AAB09784.1 .
AY254323 Genomic DNA. Translation: AAO63493.1 .
AK094575 mRNA. Translation: BAG52890.1 .
AC131159 Genomic DNA. No translation available.
BC001866 mRNA. Translation: AAH01866.1 .
BC013961 mRNA. Translation: AAH13961.1 .
CCDSi CCDS41843.2. [P40937-2 ]
CCDS9185.1. [P40937-1 ]
RefSeqi NP_001123584.1. NM_001130112.2.
NP_031396.1. NM_007370.5. [P40937-1 ]
NP_853556.2. NM_181578.3. [P40937-2 ]
UniGenei Hs.731908.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LFS model - A 1-340 [» ]
ProteinModelPortali P40937.
SMRi P40937. Positions 19-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111917. 39 interactions.
DIPi DIP-36433N.
IntActi P40937. 15 interactions.
MINTi MINT-1372754.
STRINGi 9606.ENSP00000408295.

PTM databases

PhosphoSitei P40937.

Polymorphism databases

DMDMi 728777.

Proteomic databases

MaxQBi P40937.
PaxDbi P40937.
PRIDEi P40937.

Protocols and materials databases

DNASUi 5985.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392542 ; ENSP00000376325 ; ENSG00000111445 . [P40937-2 ]
ENST00000454402 ; ENSP00000408295 ; ENSG00000111445 . [P40937-1 ]
GeneIDi 5985.
KEGGi hsa:5985.
UCSCi uc001twq.3. human. [P40937-1 ]
uc010syx.2. human. [P40937-2 ]

Organism-specific databases

CTDi 5985.
GeneCardsi GC12P118454.
HGNCi HGNC:9973. RFC5.
HPAi HPA041037.
MIMi 600407. gene.
neXtProti NX_P40937.
PharmGKBi PA34342.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0470.
GeneTreei ENSGT00550000075072.
HOGENOMi HOG000224152.
HOVERGENi HBG002053.
InParanoidi P40937.
KOi K10756.
OMAi CTGNPHP.
PhylomeDBi P40937.
TreeFami TF300810.

Enzyme and pathway databases

Reactomei REACT_1792. Polymerase switching.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_6769. Activation of ATR in response to replication stress.
REACT_7987. Polymerase switching on the C-strand of the telomere.

Miscellaneous databases

ChiTaRSi RFC5. human.
GeneWikii RFC5.
GenomeRNAii 5985.
NextBioi 23303.
PROi P40937.
SOURCEi Search...

Gene expression databases

Bgeei P40937.
CleanExi HS_RFC5.
ExpressionAtlasi P40937. baseline and differential.
Genevestigatori P40937.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C_dom.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homology in accessory proteins of replicative polymerases -- E. coli to humans."
    O'Donnell M., Onrust R., Dean F.B., Chen M., Hurwitz J.
    Nucleic Acids Res. 21:1-3(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. NIEHS SNPs program
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-13.
  3. "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 2).
    Tissue: Amygdala.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle and Skin.
  6. "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.
  7. "Purification and characterization of human DNA damage checkpoint Rad complexes."
    Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.
    Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD17.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRFC5_HUMAN
AccessioniPrimary (citable) accession number: P40937
Secondary accession number(s): A8MZ62, B3KSX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 147 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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