O75943 (RAD17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell cycle checkpoint protein RAD17
Short name=hRad17

Alternative name(s):
RF-C/activator 1 homolog

Gene names

Name:	RAD17
Synonyms:	R24L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	681 AA.
Sequence status	Complete.
Protein existence	Evidence 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.28 Ref.29 Ref.31
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
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
Sequence similarities	Belongs to the rad17/RAD24 family.

Ontologies

Keywords
Biological process	Cell cycle DNA damage
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from mutant phenotype Ref.28. Source: UniProtKB DNA repair Traceable author statement Ref.2. Source: ProtInc DNA replication Traceable author statement. Source: Reactome DNA replication checkpoint Traceable author statement Ref.2. Source: ProtInc mitotic cell cycle checkpoint Inferred from mutant phenotype Ref.28. Source: UniProtKB negative regulation of DNA replication Inferred from mutant phenotype PubMed 14657349. Source: UniProtKB regulation of phosphorylation Inferred from mutant phenotype PubMed 14657349. Source: UniProtKB
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 681	681	Cell cycle checkpoint protein RAD17		PRO_0000209948
Regions
	Nucleotide binding	137 – 144	8	ATP Potential
	Region	432 – 681	250	Interaction with MCM7
Amino acid modifications
	Modified residue	55	1	Phosphothreonine By similarity
	Modified residue	646	1	Phosphoserine; by ATR and ATM Ref.18 Ref.20 Ref.25
	Modified residue	656	1	Phosphoserine; by ATR and ATM Ref.18 Ref.20 Ref.25
Natural variations
	Alternative sequence	1 – 176	176	Missing in isoform 3.		VSP_013306
	Alternative sequence	1 – 97	97	Missing in isoform 4.		VSP_013307
	Alternative sequence	1 – 14	14	MSKTF…VSSTK → MNQ in isoform 2.		VSP_013308
	Alternative sequence	98 – 99	2	ET → MN in isoform 4.		VSP_013309
	Natural variant	32	1	V → I. Ref.13 Corresponds to variant rs17229831 [ dbSNP | Ensembl ].		VAR_021574
	Natural variant	487	1	R → L. Ref.13 Corresponds to variant rs17236478 [ dbSNP | Ensembl ].		VAR_021575
	Natural variant	535	1	K → E. Ref.13 Corresponds to variant rs17236485 [ dbSNP | Ensembl ].		VAR_021576
	Natural variant	557	1	L → R. Ref.4 Ref.13 Ref.15 Corresponds to variant rs1045051 [ dbSNP | Ensembl ].		VAR_021577
Experimental info
	Mutagenesis	143	1	K → 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.29
	Mutagenesis	143	1	K → G: Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3. Ref.17 Ref.21 Ref.29
	Mutagenesis	191	1	S → A: No effect on phosphorylation by ATR. Ref.20
	Mutagenesis	646	1	S → 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.29
	Mutagenesis	646	1	S → D: Abolishes interaction with RAD1; when associated with D-656. Ref.18 Ref.20 Ref.25 Ref.29
	Mutagenesis	656	1	S → 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.29
	Mutagenesis	656	1	S → D: Abolishes interaction with RAD1; when associated with D-646. Ref.18 Ref.20 Ref.25 Ref.29
	Sequence conflict	75	1	I → V in CAD97683. Ref.12
	Sequence conflict	187	1	F → L in AAC36334. Ref.5
	Sequence conflict	194	1	A → S in AAD01620. Ref.7
	Sequence conflict	340	1	L → P in AAC36334. Ref.5
	Sequence conflict	445	1	P → S in AAC36334. Ref.5
	Sequence conflict	462	1	M → T in AAC36334. Ref.5
	Sequence conflict	648	1	N → D in AAC36334. Ref.5
	Sequence conflict	672	1	I → M in AAC36334. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Rad17Sp) (FM2) [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 796C2BD48F7995A3	FASTA	681	77,055
	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
	Isoform 2 (Rad17Sp2) (FM1) [UniParc]. Checksum: 2C8053B065996228	FASTA	670	75,836
	10 20 30 40 50 60 MNQVTDWVDP SFDDFLECSG VSTITATSLG VNNSSHRRKN GPSTLESSRF PARKRGNLSS 70 80 90 100 110 120 LEQIYGLENS KEYLSENEPW VDKYKPETQH ELAVHKKKIE EVETWLKAQV LERQPKQGGS 130 140 150 160 170 180 ILLITGPPGC GKTTTLKILS KEHGIQVQEW INPVLPDFQK DDFKGMFNTE SSFHMFPYQS 190 200 210 220 230 240 QIAVFKEFLL RATKYNKLQM LGDDLRTDKK IILVEDLPNQ FYRDSHTLHE VLRKYVRIGR 250 260 270 280 290 300 CPLIFIISDS LSGDNNQRLL FPKEIQEECS ISNISFNPVA PTIMMKFLNR IVTIEANKNG 310 320 330 340 350 360 GKITVPDKTS LELLCQGCSG DIRSAINSLQ FSSSKGENNL RPRKKGMSLK SDAVLSKSKR 370 380 390 400 410 420 RKKPDRVFEN QEVQAIGGKD VSLFLFRALG KILYCKRASL TELDSPRLPS HLSEYERDTL 430 440 450 460 470 480 LVEPEEVVEM SHMPGDLFNL YLHQNYIDFF MEIDDIVRAS EFLSFADILS GDWNTRSLLR 490 500 510 520 530 540 EYSTSIATRG VMHSNKARGY AHCQGGGSSF RPLHKPQWFL INKKYRENCL AAKALFPDFC 550 560 570 580 590 600 LPALCLQTQL LPYLALLTIP MRNQAQISFI QDIGRLPLKR HFGRLKMEAL TDREHGMIDP 610 620 630 640 650 660 DSGDEAQLNG GHSAEESLGE PTQATVPETW SLPLSQNSAS ELPASQPQPF SAQGDMEENI 670 IIEDYESDGT
	Isoform 3 (FM3) [UniParc]. Checksum: 3F873BE5F9EF5F85	FASTA	505	57,244
	10 20 30 40 50 60 MFNTESSFHM FPYQSQIAVF KEFLLRATKY NKLQMLGDDL RTDKKIILVE DLPNQFYRDS 70 80 90 100 110 120 HTLHEVLRKY VRIGRCPLIF IISDSLSGDN NQRLLFPKEI QEECSISNIS FNPVAPTIMM 130 140 150 160 170 180 KFLNRIVTIE ANKNGGKITV PDKTSLELLC QGCSGDIRSA INSLQFSSSK GENNLRPRKK 190 200 210 220 230 240 GMSLKSDAVL SKSKRRKKPD RVFENQEVQA IGGKDVSLFL FRALGKILYC KRASLTELDS 250 260 270 280 290 300 PRLPSHLSEY ERDTLLVEPE EVVEMSHMPG DLFNLYLHQN YIDFFMEIDD IVRASEFLSF 310 320 330 340 350 360 ADILSGDWNT RSLLREYSTS IATRGVMHSN KARGYAHCQG GGSSFRPLHK PQWFLINKKY 370 380 390 400 410 420 RENCLAAKAL FPDFCLPALC LQTQLLPYLA LLTIPMRNQA QISFIQDIGR LPLKRHFGRL 430 440 450 460 470 480 KMEALTDREH GMIDPDSGDE AQLNGGHSAE ESLGEPTQAT VPETWSLPLS QNSASELPAS 490 500 QPQPFSAQGD MEENIIIEDY ESDGT
	Isoform 4 (FM4) [UniParc]. Checksum: 54FE8CE0D06C1971	FASTA	584	66,156
	10 20 30 40 50 60 MNQHELAVHK KKIEEVETWL KAQVLERQPK QGGSILLITG PPGCGKTTTL KILSKEHGIQ 70 80 90 100 110 120 VQEWINPVLP DFQKDDFKGM FNTESSFHMF PYQSQIAVFK EFLLRATKYN KLQMLGDDLR 130 140 150 160 170 180 TDKKIILVED LPNQFYRDSH TLHEVLRKYV RIGRCPLIFI ISDSLSGDNN QRLLFPKEIQ 190 200 210 220 230 240 EECSISNISF NPVAPTIMMK FLNRIVTIEA NKNGGKITVP DKTSLELLCQ GCSGDIRSAI 250 260 270 280 290 300 NSLQFSSSKG ENNLRPRKKG MSLKSDAVLS KSKRRKKPDR VFENQEVQAI GGKDVSLFLF 310 320 330 340 350 360 RALGKILYCK RASLTELDSP RLPSHLSEYE RDTLLVEPEE VVEMSHMPGD LFNLYLHQNY 370 380 390 400 410 420 IDFFMEIDDI VRASEFLSFA DILSGDWNTR SLLREYSTSI ATRGVMHSNK ARGYAHCQGG 430 440 450 460 470 480 GSSFRPLHKP QWFLINKKYR ENCLAAKALF PDFCLPALCL QTQLLPYLAL LTIPMRNQAQ 490 500 510 520 530 540 ISFIQDIGRL PLKRHFGRLK MEALTDREHG MIDPDSGDEA QLNGGHSAEE SLGEPTQATV 550 560 570 580 PETWSLPLSQ NSASELPASQ PQPFSAQGDM EENIIIEDYE SDGT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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]	"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.
[29]	"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.
[30]	"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].
[31]	"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

NIEHS-SNPs

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 , 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.
IPI	IPI00107491. IPI00107492. IPI00334267. IPI00395702.
PIR	T34548.
RefSeq	NP_002864.1. NM_002873.1. NP_579916.1. NM_133338.1. NP_579917.1. NM_133339.1. NP_579918.1. NM_133340.1. NP_579919.1. NM_133341.1. NP_579920.1. NM_133342.1. NP_579921.1. NM_133343.1. NP_579922.1. NM_133344.1.
UniGene	Hs.16184.
3D structure databases
ProteinModelPortal	O75943.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24254N. DIP-34896N.
IntAct	O75943. 3 interactions.
STRING	9606.ENSP00000370151.
PTM databases
PhosphoSite	O75943.
Proteomic databases
PaxDb	O75943.
PRIDE	O75943.
Protocols and materials databases
DNASU	5884.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000282891; ENSP00000282891; ENSG00000152942. ENST00000305138; ENSP00000303134; ENSG00000152942. ENST00000345306; ENSP00000311227; ENSG00000152942. ENST00000354312; ENSP00000346271; ENSG00000152942. ENST00000354868; ENSP00000346938; ENSG00000152942. ENST00000358030; ENSP00000350725; ENSG00000152942. ENST00000361732; ENSP00000355226; ENSG00000152942. ENST00000380774; ENSP00000370151; ENSG00000152942. ENST00000509734; ENSP00000426191; ENSG00000152942. ENST00000521422; ENSP00000427743; ENSG00000152942. ENST00000573282; ENSP00000459529; ENSG00000262511. ENST00000573405; ENSP00000461592; ENSG00000262511. ENST00000575651; ENSP00000461866; ENSG00000262511. ENST00000576047; ENSP00000458536; ENSG00000262511. ENST00000576867; ENSP00000458400; ENSG00000262511.
GeneID	5884.
KEGG	hsa:5884.
UCSC	uc003jwg.3. human. uc003jwm.3. human. uc003jwn.3. human.
Organism-specific databases
CTD	5884.
GeneCards	GC05P068700.
HGNC	HGNC:9807. RAD17.
HPA	CAB004551. HPA005448.
MIM	603139. gene.
neXtProt	NX_O75943.
PharmGKB	PA34167.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0470.
HOVERGEN	HBG059834.
InParanoid	O75943.
KO	K06662.
OMA	NYIDFFM.
OrthoDB	EOG4229J6.
PhylomeDB	O75943.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	O75943.
Bgee	O75943.
CleanEx	HS_RAD17.
Genevestigator	O75943.
GermOnline	ENSG00000152942. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR004582. Checkpoint_prot_Rad17_Rad24. IPR018324. Checkpoint_prot_Rad24_fun/met. [Graphical view]
PANTHER	PTHR12172. PTHR12172. 1 hit.
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00602. rad24. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	5884.
NextBio	22866.
SOURCE	Search...

Entry information

Entry name

RAD17_HUMAN

Accession

Primary (citable) accession number: O75943
Secondary accession number(s): A8K8X2 , 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:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.