P35251 (RFC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1148 AA.
Sequence status	Complete.
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	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 process	DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome
Cellular_component	DNA replication factor C complex Inferred from direct assay PubMed 9488738. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Traceable author statement Ref.1. Source: ProtInc DNA clamp loader activity Inferred from electronic annotation. Source: InterPro enzyme activator activity Traceable author statement PubMed 8954124. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RFC2	P35250	4	EBI-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 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 Ref.16 Ref.18

Modified residue

69

1

Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16 Ref.18

Modified residue

71

1

Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16 Ref.18

Modified residue

73

1

Phosphoserine Ref.14

Modified residue

108

1

Phosphoserine Ref.14 Ref.16

Modified residue

110

1

Phosphothreonine Ref.14 Ref.16

Modified residue

156

1

Phosphoserine Ref.14 Ref.15 Ref.16

Modified residue

161

1

Phosphothreonine Ref.14 Ref.15

Modified residue

163

1

Phosphothreonine Ref.15

Modified residue

164

1

Phosphoserine Ref.14 Ref.15

Modified residue

173

1

Phosphoserine Ref.14 Ref.15 Ref.16

Modified residue

190

1

Phosphoserine Ref.13 Ref.14 Ref.16 Ref.18

Modified residue

281

1

Phosphoserine Ref.14

Modified residue

283

1

Phosphoserine Ref.14

Modified residue

312

1

Phosphoserine Ref.14 Ref.16

Modified residue

368

1

Phosphoserine Ref.16 Ref.18

Modified residue

1104

1

Phosphoserine Ref.14

Modified residue

1106

1

Phosphoserine Ref.14

Natural variations

Alternative sequence

630

1

Missing in isoform 2.

VSP_008443

Natural variant

598

1

I → V. Ref.5
Corresponds to variant rs2066791 [ dbSNP | Ensembl ].

VAR_014860

Natural variant

613

1

R → L. Ref.2 Ref.3 Ref.4
Corresponds to variant rs1057747 [ dbSNP | Ensembl ].

VAR_016986

Natural variant

692

1

E → D. Ref.5

VAR_020657

Natural variant

955

1

Q → K. Ref.5

VAR_020658

Natural variant

1146

1

S → L. Ref.5

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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1148

Helix Strand Turn

Details...

Helix

380 – 386

7

Turn

394 – 396

3

Beta strand

404 – 407

4

Beta strand

411 – 414

4

Beta strand

419 – 421

3

Helix

423 – 432

10

Beta strand

436 – 440

5

Beta strand

447 – 450

4

Helix

457 – 465

9

Beta strand

468 – 471

4

Helix

472 – 481

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 4. Checksum: 485F0332FB56819B	FASTA	1,148	128,255
	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
	Isoform 2 [UniParc]. Checksum: D40A9F6F5CEB61AF	FASTA	1,147	128,183
	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 SSSEDKKHAK FGKFSGKDDG SSFKAALLSG PPGVGKTTTA 670 680 690 700 710 720 SLVCQELGYS YVELNASDTR SKSSLKAIVA ESLNNTSIKG FYSNGAASSV STKHALIMDE 730 740 750 760 770 780 VDGMAGNEDR GGIQELIGLI KHTKIPIICM CNDRNHPKIR SLVHYCFDLR FQRPRVEQIK 790 800 810 820 830 840 GAMMSIAFKE GLKIPPPAMN EIILGANQDI RQVLHNLSMW CARSKALTYD QAKADSHRAK 850 860 870 880 890 900 KDIKMGPFDV ARKVFAAGEE TAHMSLVDKS DLFFHDYSIA PLFVQENYIH VKPVAAGGDM 910 920 930 940 950 960 KKHLMLLSRA ADSICDGDLV DSQIRSKQNW SLLPAQAIYA SVLPGELMRG YMTQFPTFPS 970 980 990 1000 1010 1020 WLGKHSSTGK HDRIVQDLAL HMSLRTYSSK RTVNMDYLSL LRDALVQPLT SQGVDGVQDV 1030 1040 1050 1060 1070 1080 VALMDTYYLM KEDFENIMEI SSWGGKPSPF SKLDPKVKAA FTRAYNKEAH LTPYSLQAIK 1090 1100 1110 1120 1130 1140 ASRHSTSPSL DSEYNEELNE DDSQSDEKDQ DAIETDAMIK KKTKSSKPSK PEKDKEPRKG KGKSSKK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"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, MASS SPECTROMETRY.
[19]	"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

NIEHS-SNPs

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.

IPI

IPI00375358.
IPI00375359.

PIR

A49651.
JN0599.

RefSeq

NP_001191676.1. NM_001204747.1.
NP_002904.3. NM_002913.4.

UniGene

Hs.507475.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EBU	NMR	-	A	392-496	[»]
2K6G	NMR	-	A	375-480	[»]
2K7F	NMR	-	A	375-480	[»]

ProteinModelPortal

P35251.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35251. 9 interactions.

STRING

9606.ENSP00000261424.

PTM databases

PhosphoSite

P35251.

Polymorphism databases

DMDM

56757608.

Proteomic databases

PaxDb

P35251.

PRIDE

P35251.

Protocols and materials databases

DNASU

5981.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000349703; ENSP00000261424; ENSG00000035928.
ENST00000381897; ENSP00000371321; ENSG00000035928.

GeneID

5981.

KEGG

hsa:5981.

UCSC

uc003gtx.2. human.
uc003gty.2. human.

Organism-specific databases

CTD

5981.

GeneCards

GC04M039291.

HGNC

HGNC:9969. RFC1.

HPA

CAB009520.

MIM

102579. gene.

neXtProt

NX_P35251.

PharmGKB

PA34338.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5275.

HOGENOM

HOG000013116.

HOVERGEN

HBG004167.

InParanoid

P35251.

KO

K10754.

OMA

GQINFPG.

OrthoDB

EOG4D26P3.

Enzyme and pathway databases

Pathway_Interaction_DB

faspathway. FAS signaling pathway (CD95).

Reactome

REACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P35251.

Bgee

P35251.

CleanEx

HS_RFC1.

Genevestigator

P35251.

GermOnline

ENSG00000035928. Homo sapiens.

Family and domain databases

InterPro

IPR003593. 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.
[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]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF48019. Pol_clamp_load_C. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

RFC1. human.

EvolutionaryTrace

P35251.

GenomeRNAi

5981.

NextBio

23281.

PMAP-CutDB

P35251.

SOURCE

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Entry information

Entry name

RFC1_HUMAN

Accession

Primary (citable) accession number: P35251
Secondary accession number(s): A8K6E7 , Q5XKF5, Q6PKU0, Q86V41, Q86V46

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.