Reviewed, UniProtKB/Swiss-Prot P35251 (RFC1_HUMAN)

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

Name:	RFC1
Synonyms:	RFC140

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	Nucleus.
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

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	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA-dependent DNA replication Ref.1 Traceable author statement. Source: ProtInc nucleotide-excision repair, DNA gap filling Inferred from Experiment. Source: Reactome regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW telomere maintenance via telomerase Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	DNA replication factor C complex Inferred from direct assay. Source: UniProtKB nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Ref.1 Traceable author statement. Source: ProtInc DNA clamp loader activity Inferred from electronic annotation. Source: InterPro enzyme activator activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1148

Helix Strand Turn

Details...

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

	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. 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: 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. , 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: 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. , 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: 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.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PDBPDBe

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

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

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Other Resources

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:	November 24, 2009
This is version 112 of the entry and version 4 of the sequence. [Complete 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.