O60671 (RAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell cycle checkpoint protein RAD1
Short name=hRAD1
EC=3.1.11.2

Alternative name(s):
DNA repair exonuclease rad1 homolog
Rad1-like DNA damage checkpoint protein

Gene names

Name:	RAD1
Synonyms:	REC1

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	282 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity. Ref.5 Ref.30
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Subunit structure	Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD1 interacts with POLB, FEN1, HUS1, HUS1B, RAD9A and RAD9B. Interacts with DNAJC7. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28
Subcellular location	Nucleus Ref.1.
Tissue specificity	Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). Ref.1
Sequence similarities	Belongs to the rad1 family.
Sequence caution	The sequence AAC35550.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC35550.1 differs from that shown. Reason: Frameshift at position 103. The sequence CAA06249.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA06249.1 differs from that shown. Reason: Frameshift at position 103.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Exonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from mutant phenotype Ref.30. Source: UniProtKB DNA repair Traceable author statement PubMed 9872989. Source: ProtInc DNA replication Traceable author statement. Source: Reactome cellular response to ionizing radiation Inferred from direct assay Ref.30. Source: UniProtKB meiotic prophase I Traceable author statement Ref.1. Source: ProtInc
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	3'-5' exonuclease activity Inferred from direct assay Ref.5. Source: UniProtKB damaged DNA binding Non-traceable author statement Ref.5. Source: UniProtKB exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HUS1	O60921	4	EBI-721835,EBI-1056174
RAD9A	Q99638	2	EBI-721835,EBI-2606224

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60671-1)

Also known as: Hrad1A;

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: O60671-2)

Also known as: Hrad1B;

The sequence of this isoform differs from the canonical sequence as follows:
     67-102: Missing.

Isoform 3 (identifier: O60671-3)

The sequence of this isoform differs from the canonical sequence as follows:
     67-68: AG → GL
     69-282: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 282

282

Cell cycle checkpoint protein RAD1

PRO_0000225005

Natural variations

Alternative sequence

67 – 102

36

Missing in isoform 2.

VSP_017334

Alternative sequence

67 – 68

2

AG → GL in isoform 3.

VSP_017335

Alternative sequence

69 – 282

214

Missing in isoform 3.

VSP_017336

Natural variant

33

1

A → G.
Corresponds to variant rs2308951 [ dbSNP | Ensembl ].

VAR_051718

Natural variant

39

1

H → Q. Ref.11
Corresponds to variant rs41271673 [ dbSNP | Ensembl ].

VAR_055376

Natural variant

104

1

T → S.
Corresponds to variant rs1805328 [ dbSNP | Ensembl ].

VAR_051719

Natural variant

114

1

G → D.
Corresponds to variant rs2308957 [ dbSNP | Ensembl ].

VAR_051720

Natural variant

281

1

E → G. Ref.11
Corresponds to variant rs1805327 [ dbSNP | Ensembl ].

VAR_051721

Experimental info

Mutagenesis

226 – 233

8

SLLKPSTK → AAAAAAAA: Abolishes association of the 9-1-1 complex with RAD17. Ref.18

Sequence conflict

135

1

N → T in AAC95466. Ref.2

Secondary structure

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282

Helix Strand Turn

Details...

Beta strand

16 – 22

7

Helix

25 – 32

8

Beta strand

36 – 45

10

Beta strand

48 – 55

8

Turn

56 – 58

3

Beta strand

59 – 66

8

Helix

67 – 69

3

Beta strand

70 – 78

9

Beta strand

80 – 85

6

Helix

86 – 93

8

Turn

94 – 96

3

Beta strand

107 – 112

6

Beta strand

114 – 117

4

Beta strand

119 – 125

7

Beta strand

128 – 134

7

Turn

149 – 151

3

Beta strand

152 – 159

8

Helix

160 – 163

4

Helix

164 – 168

5

Beta strand

174 – 181

8

Beta strand

183 – 194

12

Beta strand

197 – 203

7

Beta strand

205 – 207

3

Beta strand

208 – 215

8

Beta strand

219 – 224

6

Helix

225 – 228

4

Helix

231 – 237

7

Beta strand

239 – 246

8

Beta strand

247 – 249

3

Beta strand

251 – 258

8

Beta strand

260 – 262

3

Beta strand

264 – 271

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Hrad1A) [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 075FBD4CF8A4FDB2	FASTA	282	31,827
	10 20 30 40 50 60 MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ 70 80 90 100 110 120 ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP MPGTLTALRM CYQGYGYPLM 130 140 150 160 170 180 LFLEEGGVVT VCKINTQEPE ETLDFDFCST NVINKIILQS EGLREAFSEL DMTSEVLQIT 190 200 210 220 230 240 MSPDKPYFRL STFGNAGSSH LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK 250 260 270 280 VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES
	Isoform 2 (Hrad1B) [UniParc]. Checksum: E96C130821B8D2D0	FASTA	246	27,828
	10 20 30 40 50 60 MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ 70 80 90 100 110 120 ANAFIQGTLT ALRMCYQGYG YPLMLFLEEG GVVTVCKINT QEPEETLDFD FCSTNVINKI 130 140 150 160 170 180 ILQSEGLREA FSELDMTSEV LQITMSPDKP YFRLSTFGNA GSSHLDYPKD SDLMEAFHCN 190 200 210 220 230 240 QTQVNRYKIS LLKPSTKALV LSCKVSIRTD NRGFLSLQYM IRNEDGQICF VEYYCCPDEE VPESES
	Isoform 3 [UniParc]. Checksum: 12B4E5E1CA5B9703	FASTA	68	7,576
	10 20 30 40 50 60 MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ ANAFIQGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis." Freire R., Murguia J.R., Tarsounas M., Lowndes N.F., Moens P.B., Jackson S.P. Genes Dev. 12:2560-2573(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell cycle checkpoint control gene." Bluyssen H.A.R., van Os R.I., Naus N.C., Jaspers I., Hoeijmakers J.H.J., de Klein A. Genomics 54:331-337(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1 cell cycle checkpoint gene." Marathi U.K., Dahlen M., Sunnerhagen P., Romero A.V., Ramagli L.S., Siciliano M.J., Li L., Legerski R.J. Genomics 54:344-347(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cervix carcinoma.
[4]	"cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster." Dean F.B., Lian L., O'Donnell M. Genomics 54:424-436(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[5]	"A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease." Parker A.E., Van de Weyer I., Laus M.C., Oostveen I., Yon J., Verhasselt P., Luyten W.H.M.L. J. Biol. Chem. 273:18332-18339(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN EXONUCLEASE ACTIVITY.
[6]	"HRAD1 and MRad1 encode mammalian homologues of the fission yeast rad1+ cell cycle checkpoint control gene." Udell C.M., Lee S.K., Davey S. Nucleic Acids Res. 26:3971-3976(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"Identification and cloning of Hrad1, a human homolog of the Schizosaccharomyces pombe checkpoint protein." Hao L., Chang M., Liu J., Chen L.B. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]	"Mammalian REC1, encoding a 3'-5' exonuclease, is differentially expressed during meiosis." Shannon M.E., Naureckiene S., Stubbs L., Holloman W.K., Thelen M.P. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[9]	"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.
[10]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[11]	NIEHS SNPs program Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-39 AND GLY-281.
[12]	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].
[13]	"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: Bone marrow, Placenta and Testis.
[14]	"Identification of novel polymorphisms in the RAD1 gene." Saegusa K.K., Suga T.K., Imai T. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 104-188 AND 223-282.
[15]	"The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1." St Onge R.P., Udell C.M., Casselman R., Davey S. Mol. Biol. Cell 10:1985-1995(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUS1 AND RAD9A.
[16]	"Physical interaction among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression." Hang H., Lieberman H.B. Genomics 65:24-33(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUS1 AND RAD9A.
[17]	"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins." Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D. J. Biol. Chem. 275:27909-27916(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1.
[18]	"The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9." Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M. J. Biol. Chem. 275:29767-29771(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17, MUTAGENESIS OF 226-SER--LYS-233.
[19]	"The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9." Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C. Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNAJC7.
[20]	"Identification and characterization of a paralog of human cell cycle checkpoint gene HUS1." Hang H., Zhang Y., Dunbrack R.L. Jr., Wang C., Lieberman H.B. Genomics 79:487-492(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUS1B.
[21]	"Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control genes in normal and cancerous testicular tissue." Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B. Cancer Res. 63:5291-5298(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAD9B.
[22]	"Identification and characterization of RAD9B, a paralog of the RAD9 checkpoint gene." Dufault V.M., Oestreich A.J., Vroman B.T., Karnitz L.M. Genomics 82:644-651(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAD9B.
[23]	"Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro." Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D., Hurwitz J., Sancar A. Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
[24]	"The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair." Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I., Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U. Nucleic Acids Res. 32:3316-3324(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB, INTERACTION WITH POLB.
[25]	"The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease 1." Wang W., Brandt P., Rossi M.L., Lindsey-Boltz L., Podust V., Fanning E., Sancar A., Bambara R.A. Proc. Natl. Acad. Sci. U.S.A. 101:16762-16767(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
[26]	"The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery." Smirnova E., Toueille M., Markkanen E., Huebscher U. Biochem. J. 389:13-17(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
[27]	"The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity." Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E., Hottiger M.O., Huebscher U. J. Mol. Biol. 353:980-989(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, INTERACTION WITH FEN1.
[28]	"Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells." Wu X., Shell S.M., Zou Y. Oncogene 24:4728-4735(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2.
[29]	"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].
[30]	"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling." Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J. Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF074717 mRNA. Translation: AAC98093.1.
AF073524 mRNA. Translation: AAC95466.1.
AF030933 mRNA. Translation: AAC95427.1.
AF076841 mRNA. Translation: AAC95523.1.
AF090170 mRNA. Translation: AAC95603.1.
AJ004974 mRNA. Translation: CAA06248.1.
AJ004975 mRNA. Translation: CAA06249.1. Sequence problems.
AF011905 mRNA. Translation: AAC27243.1.
AF058392 mRNA. Translation: AAC14138.1.
AF084512 mRNA. Translation: AAC35549.1.
AF084513 mRNA. Translation: AAC35550.1. Sequence problems.
AK002112 mRNA. Translation: BAG51017.1.
BT006908 mRNA. Translation: AAP35554.1.
DQ451401 Genomic DNA. Translation: ABD96829.1.
CH471119 Genomic DNA. Translation: EAW55904.1.
BC006837 mRNA. Translation: AAH06837.1.
BC009804 mRNA. Translation: AAH09804.1.
BC037857 mRNA. Translation: AAH37857.1.
AB183821 Genomic DNA. Translation: BAD86789.1.
AB183822 Genomic DNA. Translation: BAD86790.1.

IPI

IPI00003647.
IPI00107483.
IPI00654688.

RefSeq

NP_002844.1. NM_002853.3.

UniGene

Hs.38114.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A1J	X-ray	2.50	C	13-275	[»]
3G65	X-ray	2.90	B	1-282	[»]
3GGR	X-ray	3.20	C	1-282	[»]

ProteinModelPortal

O60671.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46061N.

IntAct

O60671. 4 interactions.

MINT

MINT-1853000.

STRING

9606.ENSP00000340879.

PTM databases

PhosphoSite

O60671.

Proteomic databases

PaxDb

O60671.

PRIDE

O60671.

Protocols and materials databases

DNASU

5810.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325577; ENSP00000313467; ENSG00000113456.
ENST00000341754; ENSP00000340879; ENSG00000113456.
ENST00000382038; ENSP00000371469; ENSG00000113456.

GeneID

5810.

KEGG

hsa:5810.

UCSC

uc003jiw.3. human.

Organism-specific databases

CTD

5810.

GeneCards

GC05M034905.

HGNC

HGNC:9806. RAD1.

HPA

HPA006692.

MIM

603153. gene.

neXtProt

NX_O60671.

PharmGKB

PA34166.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG324428.

HOGENOM

HOG000008015.

HOVERGEN

HBG053058.

InParanoid

O60671.

KO

K02830.

OMA

CKVSVRT.

OrthoDB

EOG4V9TR5.

PhylomeDB

O60671.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

O60671.

Bgee

O60671.

CleanEx

HS_RAD1.

Genevestigator

O60671.

GermOnline

ENSG00000113456. Homo sapiens.

Family and domain databases

InterPro

IPR003011. Cell_cycle_checkpoint_Rad1.
IPR003021. Rad1_Rec1_Rad17.
[Graphical view]

PANTHER

PTHR10870. PTHR10870. 1 hit.

Pfam

PF02144. Rad1. 1 hit.
[Graphical view]

PRINTS

PR01245. RAD1REC1.
PR01246. RAD1REPAIR.

ProtoNet

Search...

Other

ChiTaRS

RAD1. human.

EvolutionaryTrace

O60671.

GenomeRNAi

5810.

NextBio

22636.

SOURCE

Search...

Entry information

Entry name

RAD1_HUMAN

Accession

Primary (citable) accession number: O60671
Secondary accession number(s): O75572 , O95304, Q1W161, Q5KSM0, Q5KSM1, Q9UEP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 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.