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P35250 (RFC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 2
Alternative name(s):
Activator 1 40 kDa subunit
Short name=A1 40 kDa subunit
Activator 1 subunit 2
Replication factor C 40 kDa subunit
Short name=RF-C 40 kDa subunit
Short name=RFC40
Gene names
Name:RFC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length354 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 proliferating cell nuclear antigen (PCNA) and activator 1. This subunit binds ATP By similarity.

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. RFC2 also interacts with PRKAR1A; the complex may be involved in cell survival. Ref.9

Subcellular location

Nucleus Probable.

Involvement in disease

RFC2 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.

Sequence similarities

Belongs to the activator 1 small subunits family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseWilliams-Beuren syndrome
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

DNA replication

Traceable author statement. Source: Reactome

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Traceable author statement. Source: Reactome

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

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentDNA replication factor C complex

Inferred from direct assay PubMed 9488738. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

DNA binding

Inferred from electronic annotation. Source: InterPro

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.9PubMed 9488738. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35250-1)

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: P35250-2)

The sequence of this isoform differs from the canonical sequence as follows:
     111-144: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Replication factor C subunit 2
PRO_0000121766

Regions

Nucleotide binding76 – 838ATP Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue1631N6-acetyllysine Ref.10
Modified residue3041N6-acetyllysine Ref.10

Natural variations

Alternative sequence111 – 14434Missing in isoform 2.
VSP_005660
Natural variant2321A → V. Ref.4
Corresponds to variant rs3135684 [ dbSNP | Ensembl ].
VAR_023126

Experimental info

Sequence conflict2441G → L AA sequence Ref.1

Sequences

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

Last modified November 1, 1997. Version 3.
Checksum: B50AC8EEF89F64A9

FASTA35439,157
        10         20         30         40         50         60 
MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI VGNEDTVSRL 

        70         80         90        100        110        120 
EVFAREGNVP NIIIAGPPGT GKTTSILCLA RALLGPALKD AMLELNASND RGIDVVRNKI 

       130        140        150        160        170        180 
KMFAQQKVTL PKGRHKIIIL DEADSMTDGA QQALRRTMEI YSKTTRFALA CNASDKIIEP 

       190        200        210        220        230        240 
IQSRCAVLRY TKLTDAQILT RLMNVIEKER VPYTDDGLEA IIFTAQGDMR QALNNLQSTF 

       250        260        270        280        290        300 
SGFGFINSEN VFKVCDEPHP LLVKEMIQHC VNANIDEAYK ILAHLWHLGY SPEDIIGNIF 

       310        320        330        340        350 
RVCKTFQMAE YLKLEFIKEI GYTHMKIAEG VNSLLQMAGL LARLCQKTMA PVAS 

« Hide

Isoform 2 [UniParc].

Checksum: D6E72DD28EA014E8
Show »

FASTA32035,244

References

« Hide 'large scale' references
[1]"Sequence and expression in Escherichia coli of the 40-kDa subunit of activator 1 (replication factor C) of HeLa cells."
Chen M., Pan Z.-Q., Hurwitz J.
Proc. Natl. Acad. Sci. U.S.A. 89:2516-2520(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 232-249.
[2]Hurwitz J.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23."
Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V., Koop B.F.
Mamm. Genome 11:890-898(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[4]NIEHS SNPs program
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-232.
[5]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
[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 (SEP-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] (ISOFORM 2).
Tissue: Placenta.
[9]"The second subunit of the replication factor C complex (RFC40) and the regulatory subunit (RIalpha) of protein kinase A form a protein complex promoting cell survival."
Gupte R.S., Weng Y., Liu L., Lee M.Y.
Cell Cycle 4:323-329(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKAR1A.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163 AND LYS-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87338 mRNA. Translation: AAB09786.1.
AF045555 Genomic DNA. Translation: AAC04860.1.
AF483622 Genomic DNA. Translation: AAL82503.1.
AC005081 Genomic DNA. Translation: AAP22334.1.
AB451243 mRNA. Translation: BAG70057.1.
CH471200 Genomic DNA. Translation: EAW69607.1.
CH471200 Genomic DNA. Translation: EAW69608.1.
BC002813 mRNA. Translation: AAH02813.1.
CCDSCCDS5567.1. [P35250-2]
CCDS5568.1. [P35250-1]
PIRA42700.
RefSeqNP_001265720.1. NM_001278791.1.
NP_001265721.1. NM_001278792.1.
NP_001265722.1. NM_001278793.1.
NP_002905.2. NM_002914.4. [P35250-2]
NP_852136.1. NM_181471.2. [P35250-1]
UniGeneHs.647062.

3D structure databases

ProteinModelPortalP35250.
SMRP35250. Positions 35-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111914. 43 interactions.
DIPDIP-34367N.
IntActP35250. 13 interactions.
MINTMINT-3013724.
STRING9606.ENSP00000055077.

PTM databases

PhosphoSiteP35250.

Polymorphism databases

DMDM2507300.

Proteomic databases

MaxQBP35250.
PaxDbP35250.
PeptideAtlasP35250.
PRIDEP35250.

Protocols and materials databases

DNASU5982.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000055077; ENSP00000055077; ENSG00000049541. [P35250-1]
ENST00000352131; ENSP00000275627; ENSG00000049541. [P35250-2]
ENST00000573234; ENSP00000460590; ENSG00000261911. [P35250-2]
ENST00000576908; ENSP00000458995; ENSG00000261911. [P35250-1]
GeneID5982.
KEGGhsa:5982.
UCSCuc003uaj.3. human. [P35250-1]

Organism-specific databases

CTD5982.
GeneCardsGC07M073645.
HGNCHGNC:9970. RFC2.
HPAHPA029493.
MIM194050. phenotype.
600404. gene.
neXtProtNX_P35250.
Orphanet904. Williams syndrome.
PharmGKBPA34339.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0470.
HOGENOMHOG000224155.
HOVERGENHBG002053.
InParanoidP35250.
KOK10755.
OMAYSGTTRF.
PhylomeDBP35250.
TreeFamTF300585.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP35250.
BgeeP35250.
CleanExHS_RFC2.
GenevestigatorP35250.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C_dom.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRFC2. human.
GeneWikiRFC2.
GenomeRNAi5982.
NextBio23285.
PROP35250.
SOURCESearch...

Entry information

Entry nameRFC2_HUMAN
AccessionPrimary (citable) accession number: P35250
Secondary accession number(s): B5BU07 expand/collapse secondary AC list , D3DXG3, P32846, Q9BU93
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 153 of the entry and version 3 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

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 7

Human chromosome 7: entries, gene names and cross-references to MIM