Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P35250

- RFC2_HUMAN

UniProt

P35250 - RFC2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Replication factor C subunit 2

Gene

RFC2

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. This subunit binds ATP By similarity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 838ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: ProtInc
  2. DNA binding Source: InterPro

GO - Biological processi

  1. DNA repair Source: Reactome
  2. DNA replication Source: Reactome
  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 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 namesi
Name:RFC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9970. RFC2.

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

Involvement in diseasei

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.

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

MIMi194050. phenotype.
Orphaneti904. Williams syndrome.
PharmGKBiPA34339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Replication factor C subunit 2PRO_0000121766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei163 – 1631N6-acetyllysine1 Publication
Modified residuei304 – 3041N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP35250.
PaxDbiP35250.
PeptideAtlasiP35250.
PRIDEiP35250.

PTM databases

PhosphoSiteiP35250.

Expressioni

Gene expression databases

BgeeiP35250.
CleanExiHS_RFC2.
ExpressionAtlasiP35250. baseline and differential.
GenevestigatoriP35250.

Organism-specific databases

HPAiHPA029493.

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. RFC2 also interacts with PRKAR1A; the complex may be involved in cell survival.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKAR1AP106447EBI-476409,EBI-476431
RFC1P352514EBI-476409,EBI-476616
RFC4P352498EBI-476409,EBI-476655

Protein-protein interaction databases

BioGridi111914. 48 interactions.
DIPiDIP-34367N.
IntActiP35250. 13 interactions.
MINTiMINT-3013724.
STRINGi9606.ENSP00000055077.

Structurei

3D structure databases

ProteinModelPortaliP35250.
SMRiP35250. Positions 35-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiCOG0470.
GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
HOVERGENiHBG002053.
InParanoidiP35250.
KOiK10755.
OMAiYSGTTRF.
PhylomeDBiP35250.
TreeFamiTF300585.

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: P35250-1) [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
MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI
60 70 80 90 100
VGNEDTVSRL EVFAREGNVP NIIIAGPPGT GKTTSILCLA RALLGPALKD
110 120 130 140 150
AMLELNASND RGIDVVRNKI KMFAQQKVTL PKGRHKIIIL DEADSMTDGA
160 170 180 190 200
QQALRRTMEI YSKTTRFALA CNASDKIIEP IQSRCAVLRY TKLTDAQILT
210 220 230 240 250
RLMNVIEKER VPYTDDGLEA IIFTAQGDMR QALNNLQSTF SGFGFINSEN
260 270 280 290 300
VFKVCDEPHP LLVKEMIQHC VNANIDEAYK ILAHLWHLGY SPEDIIGNIF
310 320 330 340 350
RVCKTFQMAE YLKLEFIKEI GYTHMKIAEG VNSLLQMAGL LARLCQKTMA

PVAS
Length:354
Mass (Da):39,157
Last modified:November 1, 1997 - v3
Checksum:iB50AC8EEF89F64A9
GO
Isoform 2 (identifier: P35250-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-144: Missing.

Note: No experimental confirmation available.

Show »
Length:320
Mass (Da):35,244
Checksum:iD6E72DD28EA014E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441G → L AA sequence (PubMed:1313560)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti232 – 2321A → V.1 Publication
Corresponds to variant rs3135684 [ dbSNP | Ensembl ].
VAR_023126

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei111 – 14434Missing in isoform 2. 1 PublicationVSP_005660Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5567.1. [P35250-2]
CCDS5568.1. [P35250-1]
PIRiA42700.
RefSeqiNP_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]
UniGeneiHs.647062.

Genome annotation databases

EnsembliENST00000055077; ENSP00000055077; ENSG00000049541. [P35250-1]
ENST00000352131; ENSP00000275627; ENSG00000049541. [P35250-2]
GeneIDi5982.
KEGGihsa:5982.
UCSCiuc003uaj.3. human. [P35250-1]

Polymorphism databases

DMDMi2507300.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5567.1. [P35250-2 ]
CCDS5568.1. [P35250-1 ]
PIRi A42700.
RefSeqi NP_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 ]
UniGenei Hs.647062.

3D structure databases

ProteinModelPortali P35250.
SMRi P35250. Positions 35-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111914. 48 interactions.
DIPi DIP-34367N.
IntActi P35250. 13 interactions.
MINTi MINT-3013724.
STRINGi 9606.ENSP00000055077.

PTM databases

PhosphoSitei P35250.

Polymorphism databases

DMDMi 2507300.

Proteomic databases

MaxQBi P35250.
PaxDbi P35250.
PeptideAtlasi P35250.
PRIDEi P35250.

Protocols and materials databases

DNASUi 5982.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000055077 ; ENSP00000055077 ; ENSG00000049541 . [P35250-1 ]
ENST00000352131 ; ENSP00000275627 ; ENSG00000049541 . [P35250-2 ]
GeneIDi 5982.
KEGGi hsa:5982.
UCSCi uc003uaj.3. human. [P35250-1 ]

Organism-specific databases

CTDi 5982.
GeneCardsi GC07M073645.
HGNCi HGNC:9970. RFC2.
HPAi HPA029493.
MIMi 194050. phenotype.
600404. gene.
neXtProti NX_P35250.
Orphaneti 904. Williams syndrome.
PharmGKBi PA34339.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0470.
GeneTreei ENSGT00550000075050.
HOGENOMi HOG000224155.
HOVERGENi HBG002053.
InParanoidi P35250.
KOi K10755.
OMAi YSGTTRF.
PhylomeDBi P35250.
TreeFami TF300585.

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 RFC2. human.
GeneWikii RFC2.
GenomeRNAii 5982.
NextBioi 23285.
PROi P35250.
SOURCEi Search...

Gene expression databases

Bgeei P35250.
CleanExi HS_RFC2.
ExpressionAtlasi P35250. baseline and differential.
Genevestigatori P35250.

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. "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.
    , 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.
    , 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. 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. 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].

Entry informationi

Entry nameiRFC2_HUMAN
AccessioniPrimary (citable) accession number: P35250
Secondary accession number(s): B5BU07
, D3DXG3, P32846, Q9BU93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 156 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3