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O75943

- RAD17_HUMAN

UniProt

O75943 - RAD17_HUMAN

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Protein
Cell cycle checkpoint protein RAD17
Gene
RAD17, R24L
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination.11 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 1448ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nucleoside-triphosphatase activity Source: InterPro
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA damage checkpoint Source: UniProtKB
  2. DNA repair Source: ProtInc
  3. DNA replication Source: Reactome
  4. DNA replication checkpoint Source: ProtInc
  5. cellular response to DNA damage stimulus Source: UniProtKB
  6. mitotic cell cycle checkpoint Source: UniProtKB
  7. negative regulation of DNA replication Source: UniProtKB
  8. regulation of phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_6769. Activation of ATR in response to replication stress.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle checkpoint protein RAD17
Short name:
hRad17
Alternative name(s):
RF-C/activator 1 homolog
Gene namesi
Name:RAD17
Synonyms:R24L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9807. RAD17.

Subcellular locationi

Nucleus
Note: Phosphorylated form redistributes to discrete nuclear foci upon DNA damage.4 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431K → E: Impairs phosphorylation on S-656. Abolishes interaction with the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. 3 Publications
Mutagenesisi143 – 1431K → G: Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. 3 Publications
Mutagenesisi191 – 1911S → A: No effect on phosphorylation by ATR. 1 Publication
Mutagenesisi646 – 6461S → A: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-656. 4 Publications
Mutagenesisi646 – 6461S → D: Abolishes interaction with RAD1; when associated with D-656. 4 Publications
Mutagenesisi656 – 6561S → A: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-646. 4 Publications
Mutagenesisi656 – 6561S → D: Abolishes interaction with RAD1; when associated with D-646. 4 Publications

Organism-specific databases

PharmGKBiPA34167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681Cell cycle checkpoint protein RAD17
PRO_0000209948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551Phosphothreonine By similarity
Modified residuei646 – 6461Phosphoserine; by ATR and ATM4 Publications
Modified residuei656 – 6561Phosphoserine; by ATR and ATM3 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-646 and Ser-656 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling. Phosphorylation is mediated by ATR upon UV or replication arrest, whereas it may be mediated both by ATR and ATM upon ionizing radiation. Phosphorylation on both sites is required for interaction with RAD1 but dispensable for interaction with RFC3 or RFC4.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75943.
PaxDbiO75943.
PRIDEiO75943.

PTM databases

PhosphoSiteiO75943.

Expressioni

Tissue specificityi

Overexpressed in various cancer cell lines and in colon carcinoma (at protein level). Isoform 2 and isoform 3 are the most abundant isoforms in non irradiated cells (at protein level). Ubiquitous at low levels. Highly expressed in testis, where it is expressed within the germinal epithelium of the seminiferous tubuli. Weakly expressed in seminomas (testicular tumors).5 Publications

Inductioni

Isoform 1, isoform 3 and isoform 4 are induced by X-ray irradiation.1 Publication

Gene expression databases

ArrayExpressiO75943.
BgeeiO75943.
CleanExiHS_RAD17.
GenevestigatoriO75943.

Organism-specific databases

HPAiCAB004551.
HPA005448.

Interactioni

Subunit structurei

Part of a DNA-binding complex containing RFC2, RFC3, RFC4 and RFC5. Interacts with RAD1 and RAD9 within the RAD1-RAD9-HUS1 complex. Interacts with RAD9B, POLE, NHP2L1 and MCM7. DNA damage promotes interaction with ATR or ATM and disrupts interaction with the RAD1-RAD9-HUS1 complex.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FZR1Q9UM112EBI-968231,EBI-724997

Protein-protein interaction databases

BioGridi111821. 27 interactions.
DIPiDIP-24254N.
DIP-34896N.
IntActiO75943. 7 interactions.
MINTiMINT-3082919.
STRINGi9606.ENSP00000370151.

Structurei

3D structure databases

ProteinModelPortaliO75943.
SMRiO75943. Positions 132-158.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni432 – 681250Interaction with MCM7
Add
BLAST

Sequence similaritiesi

Belongs to the rad17/RAD24 family.

Phylogenomic databases

eggNOGiCOG0470.
HOVERGENiHBG059834.
InParanoidiO75943.
KOiK06662.
OMAiAQIAFIQ.
PhylomeDBiO75943.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR004582. Checkpoint_prot_Rad17_Rad24.
IPR018324. Checkpoint_prot_Rad24_fun/met.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR12172. PTHR12172. 1 hit.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00602. rad24. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75943-1) [UniParc]FASTAAdd to Basket

Also known as: Rad17Sp, FM2

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

MSKTFLRPKV SSTKVTDWVD PSFDDFLECS GVSTITATSL GVNNSSHRRK    50
NGPSTLESSR FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ 100
HELAVHKKKI EEVETWLKAQ VLERQPKQGG SILLITGPPG CGKTTTLKIL 150
SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT ESSFHMFPYQ SQIAVFKEFL 200
LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH EVLRKYVRIG 250
RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN 300
RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN 350
LRPRKKGMSL KSDAVLSKSK RRKKPDRVFE NQEVQAIGGK DVSLFLFRAL 400
GKILYCKRAS LTELDSPRLP SHLSEYERDT LLVEPEEVVE MSHMPGDLFN 450
LYLHQNYIDF FMEIDDIVRA SEFLSFADIL SGDWNTRSLL REYSTSIATR 500
GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENC LAAKALFPDF 550
CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA 600
LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATVPET WSLPLSQNSA 650
SELPASQPQP FSAQGDMEEN IIIEDYESDG T 681
Length:681
Mass (Da):77,055
Last modified:March 29, 2005 - v2
Checksum:i796C2BD48F7995A3
GO
Isoform 2 (identifier: O75943-2) [UniParc]FASTAAdd to Basket

Also known as: Rad17Sp2, FM1

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MSKTFLRPKVSSTK → MNQ

Show »
Length:670
Mass (Da):75,836
Checksum:i2C8053B065996228
GO
Isoform 3 (identifier: O75943-3) [UniParc]FASTAAdd to Basket

Also known as: FM3

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: Missing.

Show »
Length:505
Mass (Da):57,244
Checksum:i3F873BE5F9EF5F85
GO
Isoform 4 (identifier: O75943-4) [UniParc]FASTAAdd to Basket

Also known as: FM4

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
     98-99: ET → MN

Show »
Length:584
Mass (Da):66,156
Checksum:i54FE8CE0D06C1971
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321V → I.1 Publication
Corresponds to variant rs17229831 [ dbSNP | Ensembl ].
VAR_021574
Natural varianti487 – 4871R → L.1 Publication
Corresponds to variant rs17236478 [ dbSNP | Ensembl ].
VAR_021575
Natural varianti535 – 5351K → E.1 Publication
Corresponds to variant rs17236485 [ dbSNP | Ensembl ].
VAR_021576
Natural varianti557 – 5571L → R.3 Publications
Corresponds to variant rs1045051 [ dbSNP | Ensembl ].
VAR_021577

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 176176Missing in isoform 3.
VSP_013306Add
BLAST
Alternative sequencei1 – 9797Missing in isoform 4.
VSP_013307Add
BLAST
Alternative sequencei1 – 1414MSKTF…VSSTK → MNQ in isoform 2.
VSP_013308Add
BLAST
Alternative sequencei98 – 992ET → MN in isoform 4.
VSP_013309

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751I → V in CAD97683. 1 Publication
Sequence conflicti187 – 1871F → L in AAC36334. 1 Publication
Sequence conflicti194 – 1941A → S in AAD01620. 1 Publication
Sequence conflicti340 – 3401L → P in AAC36334. 1 Publication
Sequence conflicti445 – 4451P → S in AAC36334. 1 Publication
Sequence conflicti462 – 4621M → T in AAC36334. 1 Publication
Sequence conflicti648 – 6481N → D in AAC36334. 1 Publication
Sequence conflicti672 – 6721I → M in AAC36334. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF076838 mRNA. Translation: AAC95520.1.
AJ004977 mRNA. Translation: CAA06251.1.
AF112263 mRNA. Translation: AAD38878.1.
AF085736 mRNA. Translation: AAC36334.1.
AJ001642 mRNA. Translation: CAA04894.1.
AJ131296
, AJ131297, AJ131298, AJ131299, AJ131300, AJ131301, AJ131302, AJ131303, AJ131304, AJ131305, AJ131306, AJ131307, AJ131308 Genomic DNA. Translation: CAB46364.1.
AF017748 mRNA. Translation: AAD01620.1.
AF126424 mRNA. Translation: AAD17334.1.
AF098533 mRNA. Translation: AAC97950.1.
AF098534 mRNA. Translation: AAC97951.1.
AL122068 mRNA. Translation: CAB59244.1.
AK292487 mRNA. Translation: BAF85176.1.
BX537441 mRNA. Translation: CAD97683.1.
AY612854 Genomic DNA. Translation: AAT09763.1.
CH471137 Genomic DNA. Translation: EAW51283.1.
CH471137 Genomic DNA. Translation: EAW51284.1.
CH471137 Genomic DNA. Translation: EAW51285.1.
CH471137 Genomic DNA. Translation: EAW51286.1.
CH471137 Genomic DNA. Translation: EAW51288.1.
BC032304 mRNA. Translation: AAH32304.1.
CCDSiCCDS4003.1. [O75943-1]
CCDS4004.1. [O75943-2]
CCDS4005.1. [O75943-4]
CCDS47226.1. [O75943-3]
PIRiT34548.
RefSeqiNP_001265551.1. NM_001278622.1. [O75943-2]
NP_002864.1. NM_002873.1. [O75943-2]
NP_579916.1. NM_133338.2. [O75943-2]
NP_579917.1. NM_133339.2. [O75943-1]
NP_579918.1. NM_133340.2. [O75943-3]
NP_579919.1. NM_133341.2. [O75943-4]
NP_579920.1. NM_133342.2. [O75943-2]
NP_579921.1. NM_133343.1. [O75943-2]
NP_579922.1. NM_133344.2. [O75943-2]
UniGeneiHs.16184.

Genome annotation databases

EnsembliENST00000282891; ENSP00000282891; ENSG00000152942. [O75943-4]
ENST00000305138; ENSP00000303134; ENSG00000152942. [O75943-2]
ENST00000345306; ENSP00000311227; ENSG00000152942. [O75943-2]
ENST00000354312; ENSP00000346271; ENSG00000152942. [O75943-2]
ENST00000354868; ENSP00000346938; ENSG00000152942. [O75943-2]
ENST00000358030; ENSP00000350725; ENSG00000152942. [O75943-3]
ENST00000361732; ENSP00000355226; ENSG00000152942. [O75943-2]
ENST00000380774; ENSP00000370151; ENSG00000152942. [O75943-1]
ENST00000509734; ENSP00000426191; ENSG00000152942. [O75943-1]
ENST00000521422; ENSP00000427743; ENSG00000152942. [O75943-3]
ENST00000573282; ENSP00000459529; ENSG00000262511.
ENST00000573405; ENSP00000461592; ENSG00000262511.
ENST00000575651; ENSP00000461866; ENSG00000262511.
ENST00000576047; ENSP00000458536; ENSG00000262511.
ENST00000576867; ENSP00000458400; ENSG00000262511.
GeneIDi5884.
KEGGihsa:5884.
UCSCiuc003jwg.3. human. [O75943-2]
uc003jwm.3. human. [O75943-1]
uc003jwn.3. human. [O75943-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF076838 mRNA. Translation: AAC95520.1 .
AJ004977 mRNA. Translation: CAA06251.1 .
AF112263 mRNA. Translation: AAD38878.1 .
AF085736 mRNA. Translation: AAC36334.1 .
AJ001642 mRNA. Translation: CAA04894.1 .
AJ131296
, AJ131297 , AJ131298 , AJ131299 , AJ131300 , AJ131301 , AJ131302 , AJ131303 , AJ131304 , AJ131305 , AJ131306 , AJ131307 , AJ131308 Genomic DNA. Translation: CAB46364.1 .
AF017748 mRNA. Translation: AAD01620.1 .
AF126424 mRNA. Translation: AAD17334.1 .
AF098533 mRNA. Translation: AAC97950.1 .
AF098534 mRNA. Translation: AAC97951.1 .
AL122068 mRNA. Translation: CAB59244.1 .
AK292487 mRNA. Translation: BAF85176.1 .
BX537441 mRNA. Translation: CAD97683.1 .
AY612854 Genomic DNA. Translation: AAT09763.1 .
CH471137 Genomic DNA. Translation: EAW51283.1 .
CH471137 Genomic DNA. Translation: EAW51284.1 .
CH471137 Genomic DNA. Translation: EAW51285.1 .
CH471137 Genomic DNA. Translation: EAW51286.1 .
CH471137 Genomic DNA. Translation: EAW51288.1 .
BC032304 mRNA. Translation: AAH32304.1 .
CCDSi CCDS4003.1. [O75943-1 ]
CCDS4004.1. [O75943-2 ]
CCDS4005.1. [O75943-4 ]
CCDS47226.1. [O75943-3 ]
PIRi T34548.
RefSeqi NP_001265551.1. NM_001278622.1. [O75943-2 ]
NP_002864.1. NM_002873.1. [O75943-2 ]
NP_579916.1. NM_133338.2. [O75943-2 ]
NP_579917.1. NM_133339.2. [O75943-1 ]
NP_579918.1. NM_133340.2. [O75943-3 ]
NP_579919.1. NM_133341.2. [O75943-4 ]
NP_579920.1. NM_133342.2. [O75943-2 ]
NP_579921.1. NM_133343.1. [O75943-2 ]
NP_579922.1. NM_133344.2. [O75943-2 ]
UniGenei Hs.16184.

3D structure databases

ProteinModelPortali O75943.
SMRi O75943. Positions 132-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111821. 27 interactions.
DIPi DIP-24254N.
DIP-34896N.
IntActi O75943. 7 interactions.
MINTi MINT-3082919.
STRINGi 9606.ENSP00000370151.

PTM databases

PhosphoSitei O75943.

Proteomic databases

MaxQBi O75943.
PaxDbi O75943.
PRIDEi O75943.

Protocols and materials databases

DNASUi 5884.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282891 ; ENSP00000282891 ; ENSG00000152942 . [O75943-4 ]
ENST00000305138 ; ENSP00000303134 ; ENSG00000152942 . [O75943-2 ]
ENST00000345306 ; ENSP00000311227 ; ENSG00000152942 . [O75943-2 ]
ENST00000354312 ; ENSP00000346271 ; ENSG00000152942 . [O75943-2 ]
ENST00000354868 ; ENSP00000346938 ; ENSG00000152942 . [O75943-2 ]
ENST00000358030 ; ENSP00000350725 ; ENSG00000152942 . [O75943-3 ]
ENST00000361732 ; ENSP00000355226 ; ENSG00000152942 . [O75943-2 ]
ENST00000380774 ; ENSP00000370151 ; ENSG00000152942 . [O75943-1 ]
ENST00000509734 ; ENSP00000426191 ; ENSG00000152942 . [O75943-1 ]
ENST00000521422 ; ENSP00000427743 ; ENSG00000152942 . [O75943-3 ]
ENST00000573282 ; ENSP00000459529 ; ENSG00000262511 .
ENST00000573405 ; ENSP00000461592 ; ENSG00000262511 .
ENST00000575651 ; ENSP00000461866 ; ENSG00000262511 .
ENST00000576047 ; ENSP00000458536 ; ENSG00000262511 .
ENST00000576867 ; ENSP00000458400 ; ENSG00000262511 .
GeneIDi 5884.
KEGGi hsa:5884.
UCSCi uc003jwg.3. human. [O75943-2 ]
uc003jwm.3. human. [O75943-1 ]
uc003jwn.3. human. [O75943-4 ]

Organism-specific databases

CTDi 5884.
GeneCardsi GC05P068700.
HGNCi HGNC:9807. RAD17.
HPAi CAB004551.
HPA005448.
MIMi 603139. gene.
neXtProti NX_O75943.
PharmGKBi PA34167.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0470.
HOVERGENi HBG059834.
InParanoidi O75943.
KOi K06662.
OMAi AQIAFIQ.
PhylomeDBi O75943.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii RAD17.
GenomeRNAii 5884.
NextBioi 22866.
PROi O75943.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75943.
Bgeei O75943.
CleanExi HS_RAD17.
Genevestigatori O75943.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR004582. Checkpoint_prot_Rad17_Rad24.
IPR018324. Checkpoint_prot_Rad24_fun/met.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR12172. PTHR12172. 1 hit.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00602. rad24. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 2).
  2. "Identification of a human homologue of the Schizosaccharomyces pombe rad17+ checkpoint gene."
    Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H.M.L.
    J. Biol. Chem. 273:18340-18346(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH RAD1.
    Tissue: Neuroblastoma.
  3. Erratum
    Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H.M.L.
    J. Biol. Chem. 274:24438-24438(1999)
  4. "HRad17, a human homologue of the Schizosaccharomyces pombe checkpoint gene rad17, is overexpressed in colon carcinoma."
    Bao S., Chang M.-S., Auclair D., Sun Y., Wang Y., Wong W.-K., Zhang J., Liu Y., Qian X., Sutherland R., Magi-Galluzi C., Weisberg E., Cheng E.Y.S., Hao L., Sasaki H., Campbell M.S., Kraeft S.-K., Loda M., Lo K.-M., Chen L.B.
    Cancer Res. 59:2023-2028(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT ARG-557.
    Tissue: Fibroblast.
  5. "Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene."
    Bluyssen H.A.R., Naus N.C., van Os R.I., Jaspers I., Hoeijmakers J.H.J., de Klein A.
    Genomics 55:219-228(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
    Tissue: Thymus.
  6. "Human and mouse RAD17 genes: identification, localization, genomic structure and histological expression pattern in normal testis and seminoma."
    von Deimling F., Scharf J.M., Liehr T., Rothe M., Kelter A.-R., Albers P., Dietrich W.F., Kunkel L.M., Wernert N., Wirth B.
    Hum. Genet. 105:17-27(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  7. "hRAD17, a structural homolog of the Schizosaccharomyces pombe RAD17 cell cycle checkpoint gene, stimulates p53 accumulation."
    Li L., Peterson C.A., Kanter-Smoler G., Wei Y.-F., Ramagli L.S., Sunnerhagen P., Siciliano M.J., Legerski R.J.
    Oncogene 18:1689-1699(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
    Tissue: Cervix carcinoma.
  8. "Human hR24L gene is involved in DNA excision repair and recombination repair."
    Han Y., Zhu Y.
    Zhonghua Yi Xue Za Zhi 79:941-943(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Liver.
  9. "Multiple alternative splicing forms of human RAD17 and their differential response to ionizing radiation."
    Chen M.-S., Higashikubo R., Laszlo A., Roti Roti J.
    Gene 277:145-152(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, TISSUE SPECIFICITY.
    Tissue: Colon and Fibroblast.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  11. "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 2).
    Tissue: Testis.
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  13. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-32; LEU-487; GLU-535 AND ARG-557.
  14. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "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 2), VARIANT ARG-557.
    Tissue: Brain.
  16. "HRad17 colocalizes with NHP2L1 in the nucleolus and redistributes after UV irradiation."
    Chang M.-S., Sasaki H., Campbell M.S., Kraeft S.-K., Sutherland R., Yang C.-Y., Liu Y., Auclair D., Hao L., Sonoda H., Ferland L.H., Chen L.B.
    J. Biol. Chem. 274:36544-36549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NHP2L1.
  17. "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: INTERACTION WITH THE RAD1/RAD9/HUS1 COMPLEX AND RFC3, MUTAGENESIS OF LYS-143.
  18. "ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses."
    Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A., Chen S.M., Abraham R.T., Wang X.-F.
    Nature 411:969-974(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATM; ATR AND RAD1, PHOSPHORYLATION AT SER-646 AND SER-656, MUTAGENESIS OF SER-646 AND SER-656.
  19. "Purification and characterization of human DNA damage checkpoint Rad complexes."
    Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.
    Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH RFC2; RFC3; RFC4 AND RFC5.
  20. "Phosphorylation of serines 635 and 645 of human Rad17 is cell cycle regulated and is required for G(1)/S checkpoint activation in response to DNA damage."
    Post S.M., Weng Y.-C., Cimprich K., Chen L.B., Xu Y., Lee E.Y.-H.P.
    Proc. Natl. Acad. Sci. U.S.A. 98:13102-13107(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, INTERACTION WITH RFC4, MUTAGENESIS OF SER-191; SER-646 AND SER-656.
  21. "Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin."
    Zou L., Cortez D., Elledge S.J.
    Genes Dev. 16:198-208(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF LYS-143, SUBCELLULAR LOCATION.
  22. "Colocalization of human Rad17 and PCNA in late S phase of the cell cycle upon replication block."
    Dahm K., Huebscher U.
    Oncogene 21:7710-7719(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RFC4.
  23. "Genomic instability and endoreduplication triggered by RAD17 deletion."
    Wang X., Zou L., Zheng H., Wei Q., Elledge S.J., Li L.
    Genes Dev. 17:965-970(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "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.
  25. "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon."
    Post S.M., Tomkinson A.E., Lee E.Y.-H.P.
    Nucleic Acids Res. 31:5568-5575(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, MUTAGENESIS OF SER-646 AND SER-656, INTERACTION WITH POLE.
  26. "Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5' recessed DNA."
    Ellison V., Stillman B.
    PLoS Biol. 1:231-243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RFC2; RFC3; RFC4 AND RFC5, IDENTIFICATION BY MASS SPECTROMETRY.
  27. "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: FUNCTION, INTERACTION WITH RAD1 AND RAD9.
  28. "Requirement of protein phosphatase 5 in DNA-damage-induced ATM activation."
    Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M., Abraham R.T., Wang X.F.
    Genes Dev. 18:249-254(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP5C, PHOSPHORYLATION AT SER-646.
  29. "Interaction between human MCM7 and Rad17 proteins is required for replication checkpoint signaling."
    Tsao C.-C., Geisen C., Abraham R.T.
    EMBO J. 23:4660-4669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MCM7.
  30. "Chromatin association of rad17 is required for an ataxia telangiectasia and rad-related kinase-mediated S-phase checkpoint in response to low-dose ultraviolet radiation."
    Garg R., Callens S., Lim D.-S., Canman C.E., Kastan M.B., Xu B.
    Mol. Cancer Res. 2:362-369(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-143; SER-646 AND SER-656.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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.

Entry informationi

Entry nameiRAD17_HUMAN
AccessioniPrimary (citable) accession number: O75943
Secondary accession number(s): A8K8X2
, D3DWA5, O75714, Q7Z3S4, Q9UNK7, Q9UNR7, Q9UNR8, Q9UPF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: September 3, 2014
This is version 126 of the entry and version 2 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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