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O60671

- RAD1_HUMAN

UniProt

O60671 - RAD1_HUMAN

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Protein

Cell cycle checkpoint protein RAD1

Gene

RAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: UniProtKB
  2. damaged DNA binding Source: ProtInc
  3. exodeoxyribonuclease III activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: ProtInc
  2. cellular response to ionizing radiation Source: UniProtKB
  3. DNA damage checkpoint Source: UniProtKB
  4. DNA repair Source: ProtInc
  5. DNA replication Source: Reactome
  6. meiotic recombination checkpoint Source: UniProtKB
  7. nucleic acid phosphodiester bond hydrolysis Source: GOC
  8. substantia nigra development Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_6769. Activation of ATR in response to replication stress.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle checkpoint protein RAD1 (EC:3.1.11.2)
Short name:
hRAD1
Alternative name(s):
DNA repair exonuclease rad1 homolog
Rad1-like DNA damage checkpoint protein
Gene namesi
Name:RAD1
Synonyms:REC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9806. RAD1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. chromosome Source: UniProtKB
  2. intracellular membrane-bounded organelle Source: HPA
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi226 – 2338SLLKPSTK → AAAAAAAA: Abolishes association of the 9-1-1 complex with RAD17. 1 Publication

Organism-specific databases

PharmGKBiPA34166.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Cell cycle checkpoint protein RAD1PRO_0000225005Add
BLAST

Proteomic databases

MaxQBiO60671.
PaxDbiO60671.
PRIDEiO60671.

PTM databases

PhosphoSiteiO60671.

Expressioni

Tissue specificityi

Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level).1 Publication

Gene expression databases

BgeeiO60671.
CleanExiHS_RAD1.
ExpressionAtlasiO60671. baseline and differential.
GenevestigatoriO60671.

Organism-specific databases

HPAiHPA006692.

Interactioni

Subunit structurei

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 DNAJC7.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HUS1O609214EBI-721835,EBI-1056174
RAD9AQ996382EBI-721835,EBI-2606224

Protein-protein interaction databases

BioGridi111771. 18 interactions.
DIPiDIP-46061N.
IntActiO60671. 4 interactions.
MINTiMINT-1853000.
STRINGi9606.ENSP00000340879.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 227Combined sources
Helixi25 – 328Combined sources
Beta strandi36 – 4510Combined sources
Beta strandi48 – 558Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 668Combined sources
Helixi67 – 693Combined sources
Beta strandi70 – 789Combined sources
Beta strandi80 – 856Combined sources
Helixi86 – 938Combined sources
Turni94 – 963Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi119 – 1257Combined sources
Beta strandi128 – 1347Combined sources
Turni149 – 1513Combined sources
Beta strandi152 – 1598Combined sources
Helixi160 – 1634Combined sources
Helixi164 – 1685Combined sources
Beta strandi174 – 1818Combined sources
Beta strandi183 – 19412Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi219 – 2246Combined sources
Helixi225 – 2284Combined sources
Helixi231 – 2377Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi251 – 2588Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi264 – 2718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1JX-ray2.50C13-275[»]
3G65X-ray2.90B1-282[»]
3GGRX-ray3.20C1-282[»]
ProteinModelPortaliO60671.
SMRiO60671. Positions 13-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60671.

Family & Domainsi

Sequence similaritiesi

Belongs to the rad1 family.Curated

Phylogenomic databases

eggNOGiNOG324428.
GeneTreeiENSGT00500000044913.
HOGENOMiHOG000008015.
HOVERGENiHBG053058.
InParanoidiO60671.
KOiK02830.
OMAiCKVSVRT.
OrthoDBiEOG7N0C4P.
PhylomeDBiO60671.
TreeFamiTF101211.

Family and domain databases

InterProiIPR003011. Cell_cycle_checkpoint_Rad1.
IPR003021. Rad1_Rec1_Rad17.
[Graphical view]
PANTHERiPTHR10870. PTHR10870. 1 hit.
PfamiPF02144. Rad1. 1 hit.
[Graphical view]
PRINTSiPR01245. RAD1REC1.
PR01246. RAD1REPAIR.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60671-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK
60 70 80 90 100
VTVENAKCVQ ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP
110 120 130 140 150
MPGTLTALRM CYQGYGYPLM LFLEEGGVVT VCKINTQEPE ETLDFDFCST
160 170 180 190 200
NVINKIILQS EGLREAFSEL DMTSEVLQIT MSPDKPYFRL STFGNAGSSH
210 220 230 240 250
LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK VSIRTDNRGF
260 270 280
LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES
Length:282
Mass (Da):31,827
Last modified:August 1, 1998 - v1
Checksum:i075FBD4CF8A4FDB2
GO
Isoform 2 (identifier: O60671-2) [UniParc]FASTAAdd to Basket

Also known as: Hrad1B

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

Show »
Length:246
Mass (Da):27,828
Checksum:iE96C130821B8D2D0
GO
Isoform 3 (identifier: O60671-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:68
Mass (Da):7,576
Checksum:i12B4E5E1CA5B9703
GO

Sequence cautioni

The sequence AAC35550.1 differs from that shown. Reason: Frameshift at position 103. Curated
The sequence AAC35550.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA06249.1 differs from that shown. Reason: Frameshift at position 103. Curated
The sequence CAA06249.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351N → T in AAC95466. (PubMed:9828137)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331A → G.
Corresponds to variant rs2308951 [ dbSNP | Ensembl ].
VAR_051718
Natural varianti39 – 391H → Q.1 Publication
Corresponds to variant rs41271673 [ dbSNP | Ensembl ].
VAR_055376
Natural varianti104 – 1041T → S.
Corresponds to variant rs1805328 [ dbSNP | Ensembl ].
VAR_051719
Natural varianti114 – 1141G → D.
Corresponds to variant rs2308957 [ dbSNP | Ensembl ].
VAR_051720
Natural varianti281 – 2811E → G.1 Publication
Corresponds to variant rs1805327 [ dbSNP | Ensembl ].
VAR_051721

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei67 – 10236Missing in isoform 2. 2 PublicationsVSP_017334Add
BLAST
Alternative sequencei67 – 682AG → GL in isoform 3. 1 PublicationVSP_017335
Alternative sequencei69 – 282214Missing in isoform 3. 1 PublicationVSP_017336Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3905.1. [O60671-1]
RefSeqiNP_002844.1. NM_002853.3. [O60671-1]
UniGeneiHs.38114.

Genome annotation databases

EnsembliENST00000325577; ENSP00000313467; ENSG00000113456. [O60671-3]
ENST00000341754; ENSP00000340879; ENSG00000113456. [O60671-1]
ENST00000382038; ENSP00000371469; ENSG00000113456. [O60671-1]
GeneIDi5810.
KEGGihsa:5810.
UCSCiuc003jiw.3. human. [O60671-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS3905.1. [O60671-1 ]
RefSeqi NP_002844.1. NM_002853.3. [O60671-1 ]
UniGenei Hs.38114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali O60671.
SMRi O60671. Positions 13-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111771. 18 interactions.
DIPi DIP-46061N.
IntActi O60671. 4 interactions.
MINTi MINT-1853000.
STRINGi 9606.ENSP00000340879.

PTM databases

PhosphoSitei O60671.

Proteomic databases

MaxQBi O60671.
PaxDbi O60671.
PRIDEi O60671.

Protocols and materials databases

DNASUi 5810.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325577 ; ENSP00000313467 ; ENSG00000113456 . [O60671-3 ]
ENST00000341754 ; ENSP00000340879 ; ENSG00000113456 . [O60671-1 ]
ENST00000382038 ; ENSP00000371469 ; ENSG00000113456 . [O60671-1 ]
GeneIDi 5810.
KEGGi hsa:5810.
UCSCi uc003jiw.3. human. [O60671-1 ]

Organism-specific databases

CTDi 5810.
GeneCardsi GC05M034905.
HGNCi HGNC:9806. RAD1.
HPAi HPA006692.
MIMi 603153. gene.
neXtProti NX_O60671.
PharmGKBi PA34166.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324428.
GeneTreei ENSGT00500000044913.
HOGENOMi HOG000008015.
HOVERGENi HBG053058.
InParanoidi O60671.
KOi K02830.
OMAi CKVSVRT.
OrthoDBi EOG7N0C4P.
PhylomeDBi O60671.
TreeFami TF101211.

Enzyme and pathway databases

Reactomei REACT_6769. Activation of ATR in response to replication stress.

Miscellaneous databases

ChiTaRSi RAD1. human.
EvolutionaryTracei O60671.
GeneWikii RAD1_homolog.
GenomeRNAii 5810.
NextBioi 22636.
PROi O60671.
SOURCEi Search...

Gene expression databases

Bgeei O60671.
CleanExi HS_RAD1.
ExpressionAtlasi O60671. baseline and differential.
Genevestigatori O60671.

Family and domain databases

InterProi IPR003011. Cell_cycle_checkpoint_Rad1.
IPR003021. Rad1_Rec1_Rad17.
[Graphical view ]
PANTHERi PTHR10870. PTHR10870. 1 hit.
Pfami PF02144. Rad1. 1 hit.
[Graphical view ]
PRINTSi PR01245. RAD1REC1.
PR01246. RAD1REPAIR.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAD1_HUMAN
AccessioniPrimary (citable) accession number: O60671
Secondary accession number(s): O75572
, O95304, Q1W161, Q5KSM0, Q5KSM1, Q9UEP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3