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O75943 (RAD17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 RAD17

Short name=hRad17
Alternative name(s):
RF-C/activator 1 homolog
Gene names
Name:RAD17
Synonyms:R24L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length681 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.18 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32

Subunit structure

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. Ref.2 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29

Subcellular location

Nucleus. Note: Phosphorylated form redistributes to discrete nuclear foci upon DNA damage. Ref.4 Ref.16 Ref.21 Ref.22

Tissue specificity

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). Ref.2 Ref.4 Ref.6 Ref.7 Ref.9

Induction

Isoform 1, isoform 3 and isoform 4 are induced by X-ray irradiation. Ref.9

Post-translational modification

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. Ref.18 Ref.20 Ref.21 Ref.25 Ref.28

Sequence similarities

Belongs to the rad17/RAD24 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FZR1Q9UM112EBI-968231,EBI-724997

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75943-1)

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.
Isoform 2 (identifier: O75943-2)

Also known as: Rad17Sp2; FM1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MSKTFLRPKVSSTK → MNQ
Isoform 3 (identifier: O75943-3)

Also known as: FM3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: Missing.
Isoform 4 (identifier: O75943-4)

Also known as: FM4;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 681681Cell cycle checkpoint protein RAD17
PRO_0000209948

Regions

Nucleotide binding137 – 1448ATP Potential
Region432 – 681250Interaction with MCM7

Amino acid modifications

Modified residue551Phosphothreonine By similarity
Modified residue6461Phosphoserine; by ATR and ATM Ref.18 Ref.20 Ref.25 Ref.28
Modified residue6561Phosphoserine; by ATR and ATM Ref.18 Ref.20 Ref.25

Natural variations

Alternative sequence1 – 176176Missing in isoform 3.
VSP_013306
Alternative sequence1 – 9797Missing in isoform 4.
VSP_013307
Alternative sequence1 – 1414MSKTF…VSSTK → MNQ in isoform 2.
VSP_013308
Alternative sequence98 – 992ET → MN in isoform 4.
VSP_013309
Natural variant321V → I. Ref.13
Corresponds to variant rs17229831 [ dbSNP | Ensembl ].
VAR_021574
Natural variant4871R → L. Ref.13
Corresponds to variant rs17236478 [ dbSNP | Ensembl ].
VAR_021575
Natural variant5351K → E. Ref.13
Corresponds to variant rs17236485 [ dbSNP | Ensembl ].
VAR_021576
Natural variant5571L → R. Ref.4 Ref.13 Ref.15
Corresponds to variant rs1045051 [ dbSNP | Ensembl ].
VAR_021577

Experimental info

Mutagenesis1431K → E: Impairs phosphorylation on S-656. Abolishes interaction with the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. Ref.17 Ref.21 Ref.30
Mutagenesis1431K → G: Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. Ref.17 Ref.21 Ref.30
Mutagenesis1911S → A: No effect on phosphorylation by ATR. Ref.20
Mutagenesis6461S → 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. Ref.18 Ref.20 Ref.25 Ref.30
Mutagenesis6461S → D: Abolishes interaction with RAD1; when associated with D-656. Ref.18 Ref.20 Ref.25 Ref.30
Mutagenesis6561S → 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. Ref.18 Ref.20 Ref.25 Ref.30
Mutagenesis6561S → D: Abolishes interaction with RAD1; when associated with D-646. Ref.18 Ref.20 Ref.25 Ref.30
Sequence conflict751I → V in CAD97683. Ref.12
Sequence conflict1871F → L in AAC36334. Ref.5
Sequence conflict1941A → S in AAD01620. Ref.7
Sequence conflict3401L → P in AAC36334. Ref.5
Sequence conflict4451P → S in AAC36334. Ref.5
Sequence conflict4621M → T in AAC36334. Ref.5
Sequence conflict6481N → D in AAC36334. Ref.5
Sequence conflict6721I → M in AAC36334. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Rad17Sp) (FM2) [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 796C2BD48F7995A3

FASTA68177,055
        10         20         30         40         50         60 
MSKTFLRPKV SSTKVTDWVD PSFDDFLECS GVSTITATSL GVNNSSHRRK NGPSTLESSR 

        70         80         90        100        110        120 
FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ HELAVHKKKI EEVETWLKAQ 

       130        140        150        160        170        180 
VLERQPKQGG SILLITGPPG CGKTTTLKIL SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT 

       190        200        210        220        230        240 
ESSFHMFPYQ SQIAVFKEFL LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH 

       250        260        270        280        290        300 
EVLRKYVRIG RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN 

       310        320        330        340        350        360 
RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN LRPRKKGMSL 

       370        380        390        400        410        420 
KSDAVLSKSK RRKKPDRVFE NQEVQAIGGK DVSLFLFRAL GKILYCKRAS LTELDSPRLP 

       430        440        450        460        470        480 
SHLSEYERDT LLVEPEEVVE MSHMPGDLFN LYLHQNYIDF FMEIDDIVRA SEFLSFADIL 

       490        500        510        520        530        540 
SGDWNTRSLL REYSTSIATR GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENC 

       550        560        570        580        590        600 
LAAKALFPDF CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA 

       610        620        630        640        650        660 
LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATVPET WSLPLSQNSA SELPASQPQP 

       670        680 
FSAQGDMEEN IIIEDYESDG T 

« Hide

Isoform 2 (Rad17Sp2) (FM1) [UniParc].

Checksum: 2C8053B065996228
Show »

FASTA67075,836
Isoform 3 (FM3) [UniParc].

Checksum: 3F873BE5F9EF5F85
Show »

FASTA50557,244
Isoform 4 (FM4) [UniParc].

Checksum: 54FE8CE0D06C1971
Show »

FASTA58466,156

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. 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 2).
Tissue: Testis.
[12]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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].
[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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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.
CCDSCCDS4003.1. [O75943-1]
CCDS4004.1. [O75943-2]
CCDS4005.1. [O75943-4]
CCDS47226.1. [O75943-3]
PIRT34548.
RefSeqNP_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]
UniGeneHs.16184.

3D structure databases

ProteinModelPortalO75943.
SMRO75943. Positions 132-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111821. 27 interactions.
DIPDIP-24254N.
DIP-34896N.
IntActO75943. 7 interactions.
MINTMINT-3082919.
STRING9606.ENSP00000370151.

PTM databases

PhosphoSiteO75943.

Proteomic databases

MaxQBO75943.
PaxDbO75943.
PRIDEO75943.

Protocols and materials databases

DNASU5884.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282891; 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.
GeneID5884.
KEGGhsa:5884.
UCSCuc003jwg.3. human. [O75943-2]
uc003jwm.3. human. [O75943-1]
uc003jwn.3. human. [O75943-4]

Organism-specific databases

CTD5884.
GeneCardsGC05P068700.
HGNCHGNC:9807. RAD17.
HPACAB004551.
HPA005448.
MIM603139. gene.
neXtProtNX_O75943.
PharmGKBPA34167.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0470.
HOVERGENHBG059834.
InParanoidO75943.
KOK06662.
OMAAQIAFIQ.
PhylomeDBO75943.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO75943.
BgeeO75943.
CleanExHS_RAD17.
GenevestigatorO75943.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR004582. Checkpoint_prot_Rad17_Rad24.
IPR018324. Checkpoint_prot_Rad24_fun/met.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR12172. PTHR12172. 1 hit.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00602. rad24. 1 hit.
ProtoNetSearch...

Other

GeneWikiRAD17.
GenomeRNAi5884.
NextBio22866.
PROO75943.
SOURCESearch...

Entry information

Entry nameRAD17_HUMAN
AccessionPrimary (citable) accession number: O75943
Secondary accession number(s): A8K8X2 expand/collapse secondary AC list , D3DWA5, O75714, Q7Z3S4, Q9UNK7, Q9UNR7, Q9UNR8, Q9UPF5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 125 of the entry and version 2 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

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