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O60671 (RAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionExonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

cell cycle checkpoint

Non-traceable author statement Ref.5. Source: UniProtKB

cellular response to DNA damage stimulus

Traceable author statement PubMed 9872989. Source: ProtInc

cellular response to ionizing radiation

Inferred from direct assay Ref.30. Source: UniProtKB

meiotic prophase I

Traceable author statement Ref.1. Source: ProtInc

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay Ref.5. Source: GOC

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred by curator Ref.5. Source: UniProtKB

   Molecular_function3'-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: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Cell cycle checkpoint protein RAD1
PRO_0000225005

Natural variations

Alternative sequence67 – 10236Missing in isoform 2.
VSP_017334
Alternative sequence67 – 682AG → GL in isoform 3.
VSP_017335
Alternative sequence69 – 282214Missing in isoform 3.
VSP_017336
Natural variant331A → G.
Corresponds to variant rs2308951 [ dbSNP | Ensembl ].
VAR_051718
Natural variant391H → Q. Ref.11
Corresponds to variant rs41271673 [ dbSNP | Ensembl ].
VAR_055376
Natural variant1041T → S.
Corresponds to variant rs1805328 [ dbSNP | Ensembl ].
VAR_051719
Natural variant1141G → D.
Corresponds to variant rs2308957 [ dbSNP | Ensembl ].
VAR_051720
Natural variant2811E → G. Ref.11
Corresponds to variant rs1805327 [ dbSNP | Ensembl ].
VAR_051721

Experimental info

Mutagenesis226 – 2338SLLKPSTK → AAAAAAAA: Abolishes association of the 9-1-1 complex with RAD17. Ref.18
Sequence conflict1351N → T in AAC95466. Ref.2

Secondary structure

..................................................... 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Hrad1A) [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 075FBD4CF8A4FDB2

FASTA28231,827
        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 

« Hide

Isoform 2 (Hrad1B) [UniParc].

Checksum: E96C130821B8D2D0
Show »

FASTA24627,828
Isoform 3 [UniParc].

Checksum: 12B4E5E1CA5B9703
Show »

FASTA687,576

References

« Hide '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. expand/collapse author list , 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. 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 (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.
[31]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

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.
CCDSCCDS3905.1. [O60671-1]
RefSeqNP_002844.1. NM_002853.3. [O60671-1]
UniGeneHs.38114.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1JX-ray2.50C13-275[»]
3G65X-ray2.90B1-282[»]
3GGRX-ray3.20C1-282[»]
ProteinModelPortalO60671.
SMRO60671. Positions 13-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111771. 16 interactions.
DIPDIP-46061N.
IntActO60671. 4 interactions.
MINTMINT-1853000.
STRING9606.ENSP00000340879.

PTM databases

PhosphoSiteO60671.

Proteomic databases

MaxQBO60671.
PaxDbO60671.
PRIDEO60671.

Protocols and materials databases

DNASU5810.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325577; ENSP00000313467; ENSG00000113456. [O60671-3]
ENST00000341754; ENSP00000340879; ENSG00000113456. [O60671-1]
ENST00000382038; ENSP00000371469; ENSG00000113456. [O60671-1]
GeneID5810.
KEGGhsa:5810.
UCSCuc003jiw.3. human. [O60671-1]

Organism-specific databases

CTD5810.
GeneCardsGC05M034905.
HGNCHGNC:9806. RAD1.
HPAHPA006692.
MIM603153. gene.
neXtProtNX_O60671.
PharmGKBPA34166.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324428.
HOGENOMHOG000008015.
HOVERGENHBG053058.
InParanoidO60671.
KOK02830.
OMACKVSVRT.
OrthoDBEOG7N0C4P.
PhylomeDBO60671.
TreeFamTF101211.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO60671.
BgeeO60671.
CleanExHS_RAD1.
GenevestigatorO60671.

Family and domain databases

InterProIPR003011. Cell_cycle_checkpoint_Rad1.
IPR003021. Rad1_Rec1_Rad17.
[Graphical view]
PANTHERPTHR10870. PTHR10870. 1 hit.
PfamPF02144. Rad1. 1 hit.
[Graphical view]
PRINTSPR01245. RAD1REC1.
PR01246. RAD1REPAIR.
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Other

ChiTaRSRAD1. human.
EvolutionaryTraceO60671.
GeneWikiRAD1_homolog.
GenomeRNAi5810.
NextBio22636.
PROO60671.
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Entry information

Entry nameRAD1_HUMAN
AccessionPrimary (citable) accession number: O60671
Secondary accession number(s): O75572 expand/collapse secondary AC list , O95304, Q1W161, Q5KSM0, Q5KSM1, Q9UEP1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 120 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 5

Human chromosome 5: entries, gene names and cross-references to MIM