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Protein

Checkpoint protein HUS1

Gene

HUS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage

Enzyme and pathway databases

BRENDAi2.3.2.B10. 2681.
ReactomeiREACT_6769. Activation of ATR in response to replication stress.
SignaLinkiO60921.

Names & Taxonomyi

Protein namesi
Recommended name:
Checkpoint protein HUS1
Short name:
hHUS1
Gene namesi
Name:HUS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:5309. HUS1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: In discrete nuclear foci upon DNA damage. According to PubMed:14500360, localized also in the cytoplasm. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm.

GO - Cellular componenti

  • checkpoint clamp complex Source: GO_Central
  • cytoplasm Source: UniProtKB-SubCell
  • nucleolus Source: InterPro
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • site of double-strand break Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29564.

Polymorphism and mutation databases

BioMutaiHUS1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Checkpoint protein HUS1PRO_0000225003Add
BLAST

Proteomic databases

MaxQBiO60921.
PaxDbiO60921.
PRIDEiO60921.

PTM databases

PhosphoSiteiO60921.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO60921.
CleanExiHS_HUS1.
ExpressionAtlasiO60921. baseline and differential.
GenevisibleiO60921. HS.

Organism-specific databases

HPAiHPA026787.

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. HUS1 interacts with POLB, HDAC1, FEN1, PCNA, RAD1, RAD9A and RAD9B. HUS1 does not interact with RAD17. Interacts with DNAJC7.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD1O606714EBI-1056174,EBI-721835
RAD9AQ996385EBI-1056174,EBI-2606224

Protein-protein interaction databases

BioGridi109596. 29 interactions.
DIPiDIP-40929N.
IntActiO60921. 4 interactions.
MINTiMINT-134822.
STRINGi9606.ENSP00000258774.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi10 – 2617Combined sources
Beta strandi28 – 347Combined sources
Beta strandi36 – 438Combined sources
Beta strandi46 – 483Combined sources
Beta strandi53 – 597Combined sources
Helixi60 – 623Combined sources
Beta strandi65 – 706Combined sources
Beta strandi72 – 743Combined sources
Beta strandi79 – 846Combined sources
Helixi85 – 917Combined sources
Helixi92 – 976Combined sources
Beta strandi98 – 1069Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi112 – 1198Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi135 – 1373Combined sources
Helixi140 – 1467Combined sources
Beta strandi155 – 1595Combined sources
Helixi163 – 17412Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi228 – 2336Combined sources
Helixi234 – 24310Combined sources
Beta strandi249 – 2568Combined sources
Turni257 – 2593Combined sources
Beta strandi260 – 26910Combined sources
Beta strandi271 – 2777Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1JX-ray2.50B1-280[»]
3G65X-ray2.90C1-280[»]
3GGRX-ray3.20B2-280[»]
ProteinModelPortaliO60921.
SMRiO60921. Positions 3-280.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60921.

Family & Domainsi

Sequence similaritiesi

Belongs to the HUS1 family.Curated

Phylogenomic databases

eggNOGiNOG250864.
GeneTreeiENSGT00390000000706.
HOGENOMiHOG000253011.
HOVERGENiHBG053069.
InParanoidiO60921.
KOiK10903.
OMAiCMILYVY.
PhylomeDBiO60921.
TreeFamiTF314491.

Family and domain databases

InterProiIPR016580. Cell_cycle_HUS1.
IPR007150. Hus1/Mec3.
[Graphical view]
PANTHERiPTHR12900. PTHR12900. 1 hit.
PfamiPF04005. Hus1. 1 hit.
[Graphical view]
PIRSFiPIRSF011312. Cell_cycle_HUS1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60921-1) [UniParc]FASTAAdd to basket

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
MKFRAKIVDG ACLNHFTRIS NMIAKLAKTC TLRISPDKLN FILCDKLANG
60 70 80 90 100
GVSMWCELEQ ENFFNEFQME GVSAENNEIY LELTSENLSR ALKTAQNARA
110 120 130 140 150
LKIKLTNKHF PCLTVSVELL SMSSSSRIVT HDIPIKVIPR KLWKDLQEPV
160 170 180 190 200
VPDPDVSIYL PVLKTMKSVV EKMKNISNHL VIEANLDGEL NLKIETELVC
210 220 230 240 250
VTTHFKDLGN PPLASESTHE DRNVEHMAEV HIDIRKLLQF LAGQQVNPTK
260 270 280
ALCNIVNNKM VHFDLLHEDV SLQYFIPALS
Length:280
Mass (Da):31,691
Last modified:August 1, 1998 - v1
Checksum:i9C3ED2FD35C2ACB3
GO
Isoform 2 (identifier: O60921-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: No experimental confirmation available.
Show »
Length:259
Mass (Da):29,287
Checksum:iD97AE567F923089B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261S → G.
Corresponds to variant rs2307261 [ dbSNP | Ensembl ].
VAR_033999
Natural varianti147 – 1471Q → K.1 Publication
Corresponds to variant rs2307254 [ dbSNP | Ensembl ].
VAR_025414
Natural varianti221 – 2211D → E.1 Publication
Corresponds to variant rs3176588 [ dbSNP | Ensembl ].
VAR_025415

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_056702Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16893 mRNA. Translation: CAA76518.1.
AF076844 mRNA. Translation: AAC95526.1.
AF110393 mRNA. Translation: AAD25350.1.
AK294117 mRNA. Translation: BAG57450.1.
AC019066 Genomic DNA. No translation available.
AC069282 Genomic DNA. No translation available.
AC104696 Genomic DNA. No translation available.
CR536552 mRNA. Translation: CAG38789.1.
BT019481 mRNA. Translation: AAV38288.1.
BT019482 mRNA. Translation: AAV38289.1.
AF503165 Genomic DNA. Translation: AAM18968.1.
BC007013 mRNA. Translation: AAH07013.1.
CCDSiCCDS34635.1. [O60921-1]
RefSeqiNP_004498.1. NM_004507.3. [O60921-1]
UniGeneiHs.152983.

Genome annotation databases

EnsembliENST00000258774; ENSP00000258774; ENSG00000136273. [O60921-1]
ENST00000432325; ENSP00000416588; ENSG00000136273. [O60921-2]
ENST00000436444; ENSP00000403844; ENSG00000136273. [O60921-1]
ENST00000458191; ENSP00000400727; ENSG00000136273. [O60921-2]
GeneIDi3364.
KEGGihsa:3364.
UCSCiuc003tod.2. human. [O60921-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16893 mRNA. Translation: CAA76518.1.
AF076844 mRNA. Translation: AAC95526.1.
AF110393 mRNA. Translation: AAD25350.1.
AK294117 mRNA. Translation: BAG57450.1.
AC019066 Genomic DNA. No translation available.
AC069282 Genomic DNA. No translation available.
AC104696 Genomic DNA. No translation available.
CR536552 mRNA. Translation: CAG38789.1.
BT019481 mRNA. Translation: AAV38288.1.
BT019482 mRNA. Translation: AAV38289.1.
AF503165 Genomic DNA. Translation: AAM18968.1.
BC007013 mRNA. Translation: AAH07013.1.
CCDSiCCDS34635.1. [O60921-1]
RefSeqiNP_004498.1. NM_004507.3. [O60921-1]
UniGeneiHs.152983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1JX-ray2.50B1-280[»]
3G65X-ray2.90C1-280[»]
3GGRX-ray3.20B2-280[»]
ProteinModelPortaliO60921.
SMRiO60921. Positions 3-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109596. 29 interactions.
DIPiDIP-40929N.
IntActiO60921. 4 interactions.
MINTiMINT-134822.
STRINGi9606.ENSP00000258774.

PTM databases

PhosphoSiteiO60921.

Polymorphism and mutation databases

BioMutaiHUS1.

Proteomic databases

MaxQBiO60921.
PaxDbiO60921.
PRIDEiO60921.

Protocols and materials databases

DNASUi3364.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258774; ENSP00000258774; ENSG00000136273. [O60921-1]
ENST00000432325; ENSP00000416588; ENSG00000136273. [O60921-2]
ENST00000436444; ENSP00000403844; ENSG00000136273. [O60921-1]
ENST00000458191; ENSP00000400727; ENSG00000136273. [O60921-2]
GeneIDi3364.
KEGGihsa:3364.
UCSCiuc003tod.2. human. [O60921-1]

Organism-specific databases

CTDi3364.
GeneCardsiGC07M047735.
H-InvDBHIX0033836.
HGNCiHGNC:5309. HUS1.
HPAiHPA026787.
MIMi603760. gene.
neXtProtiNX_O60921.
PharmGKBiPA29564.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250864.
GeneTreeiENSGT00390000000706.
HOGENOMiHOG000253011.
HOVERGENiHBG053069.
InParanoidiO60921.
KOiK10903.
OMAiCMILYVY.
PhylomeDBiO60921.
TreeFamiTF314491.

Enzyme and pathway databases

BRENDAi2.3.2.B10. 2681.
ReactomeiREACT_6769. Activation of ATR in response to replication stress.
SignaLinkiO60921.

Miscellaneous databases

EvolutionaryTraceiO60921.
GeneWikiiHUS1.
GenomeRNAii3364.
NextBioi13320.
PROiO60921.
SOURCEiSearch...

Gene expression databases

BgeeiO60921.
CleanExiHS_HUS1.
ExpressionAtlasiO60921. baseline and differential.
GenevisibleiO60921. HS.

Family and domain databases

InterProiIPR016580. Cell_cycle_HUS1.
IPR007150. Hus1/Mec3.
[Graphical view]
PANTHERiPTHR12900. PTHR12900. 1 hit.
PfamiPF04005. Hus1. 1 hit.
[Graphical view]
PIRSFiPIRSF011312. Cell_cycle_HUS1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Hus1p, a conserved fission yeast checkpoint protein, interacts with Rad1p and is phosphorylated in response to DNA damage."
    Kostrub C.F., Knudsen K., Subramani S., Enoch T.
    EMBO J. 17:2055-2066(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 1).
  3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RAD1 AND RAD9A, TISSUE SPECIFICITY.
    Tissue: T-cell.
  4. "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).
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. NIEHS SNPs program
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-147 AND GLU-221.
  8. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Urinary bladder.
  10. "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 RAD1 AND RAD9A.
  11. "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, INTERACTION WITH HDAC1, SUBCELLULAR LOCATION.
  12. "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.
  13. "PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition."
    Komatsu K., Wharton W., Hang H., Wu C., Singh S., Lieberman H.B., Pledger W.J., Wang H.-G.
    Oncogene 19:5291-5297(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
  14. "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.
  15. "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.
  16. "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.
  17. "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, LACK OF INTERACTION WITH RAD17, ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
  18. "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.
  19. Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
  20. "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.
  21. "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.
  22. "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.
  23. "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.

Entry informationi

Entry nameiHUS1_HUMAN
AccessioniPrimary (citable) accession number: O60921
Secondary accession number(s): B4DFI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: August 1, 1998
Last modified: June 24, 2015
This is version 118 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 7
    Human chromosome 7: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.