HUS1_MOUSE
ID HUS1_MOUSE Reviewed; 280 AA.
AC Q8BQY8; O70543; Q6P8H5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Checkpoint protein HUS1;
DE Short=mHUS1;
GN Name=Hus1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9878245; DOI=10.1006/geno.1998.5587;
RA Dean F.B., Lian L., O'Donnell M.;
RT "cDNA cloning and gene mapping of human homologs for Schizosaccharomyces
RT pombe rad17, rad1, and hus1 and cloning of homologs from mouse,
RT Caenorhabditis elegans, and Drosophila melanogaster.";
RL Genomics 54:424-436(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=10395797; DOI=10.1006/geno.1999.5865;
RA Weiss R.S., Kostrub C.F., Enoch T., Leder P.;
RT "Mouse Hus1, a homologue of the Schizosaccharomyces pombe hus1+ cell cycle
RT checkpoint gene.";
RL Genomics 59:32-39(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, Egg, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
CC that plays a major role in DNA repair. The 9-1-1 complex is recruited
CC to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp
CC loader complex. Acts then as a sliding clamp platform on DNA for
CC several proteins involved in long-patch base excision repair (LP-BER).
CC The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by
CC increasing its affinity for the 3'-OH end of the primer-template and
CC stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1
CC cleavage activity on substrates with double, nick, or gap flaps of
CC distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch
CC base excision repair substrates. The 9-1-1 complex is necessary for the
CC recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring
CC during the S phase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
CC composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with
CC LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex
CC associates with the RAD17-RFC complex. HUS1 interacts with POLB, HDAC1,
CC FEN1, PCNA, RAD1, RAD9A and RAD9B. HUS1 does not interact with RAD17.
CC Interacts with DNAJC7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60921}. Cytoplasm
CC {ECO:0000250|UniProtKB:O60921}. Note=In discrete nuclear foci upon DNA
CC damage. DNA damage induces its nuclear translocation. Shuttles between
CC the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:O60921}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BQY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BQY8-2; Sequence=VSP_017332;
CC Name=3;
CC IsoId=Q8BQY8-3; Sequence=VSP_017332, VSP_017333;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10395797}.
CC -!- SIMILARITY: Belongs to the HUS1 family. {ECO:0000305}.
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DR EMBL; Y16894; CAA76519.1; -; mRNA.
DR EMBL; AF076845; AAC95527.1; -; mRNA.
DR EMBL; AK046152; BAC32614.1; -; mRNA.
DR EMBL; AK088403; BAC40332.1; -; mRNA.
DR EMBL; AK135922; BAE22725.1; -; mRNA.
DR EMBL; AL669837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061249; AAH61249.1; -; mRNA.
DR CCDS; CCDS24429.1; -. [Q8BQY8-2]
DR RefSeq; NP_001290461.1; NM_001303532.1. [Q8BQY8-1]
DR RefSeq; NP_032342.1; NM_008316.5. [Q8BQY8-2]
DR RefSeq; XP_006514594.1; XM_006514531.3. [Q8BQY8-3]
DR AlphaFoldDB; Q8BQY8; -.
DR SMR; Q8BQY8; -.
DR BioGRID; 200488; 3.
DR STRING; 10090.ENSMUSP00000020683; -.
DR PhosphoSitePlus; Q8BQY8; -.
DR EPD; Q8BQY8; -.
DR MaxQB; Q8BQY8; -.
DR PaxDb; Q8BQY8; -.
DR PeptideAtlas; Q8BQY8; -.
DR PRIDE; Q8BQY8; -.
DR ProteomicsDB; 273204; -. [Q8BQY8-1]
DR ProteomicsDB; 273205; -. [Q8BQY8-2]
DR ProteomicsDB; 273206; -. [Q8BQY8-3]
DR Antibodypedia; 27543; 261 antibodies from 30 providers.
DR DNASU; 15574; -.
DR Ensembl; ENSMUST00000020683; ENSMUSP00000020683; ENSMUSG00000020413. [Q8BQY8-2]
DR Ensembl; ENSMUST00000129115; ENSMUSP00000114339; ENSMUSG00000020413. [Q8BQY8-2]
DR GeneID; 15574; -.
DR KEGG; mmu:15574; -.
DR UCSC; uc007hzp.2; mouse. [Q8BQY8-1]
DR UCSC; uc007hzq.2; mouse. [Q8BQY8-2]
DR UCSC; uc007hzs.2; mouse. [Q8BQY8-3]
DR CTD; 3364; -.
DR MGI; MGI:1277962; Hus1.
DR VEuPathDB; HostDB:ENSMUSG00000020413; -.
DR eggNOG; KOG3999; Eukaryota.
DR GeneTree; ENSGT00390000000706; -.
DR HOGENOM; CLU_035754_1_0_1; -.
DR InParanoid; Q8BQY8; -.
DR OMA; PWASEDG; -.
DR OrthoDB; 1053181at2759; -.
DR PhylomeDB; Q8BQY8; -.
DR TreeFam; TF314491; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 15574; 28 hits in 111 CRISPR screens.
DR ChiTaRS; Hus1; mouse.
DR PRO; PR:Q8BQY8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BQY8; protein.
DR Bgee; ENSMUSG00000020413; Expressed in secondary oocyte and 259 other tissues.
DR Genevisible; Q8BQY8; MM.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0044778; P:meiotic DNA integrity checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:MGI.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR InterPro; IPR016580; Cell_cycle_HUS1.
DR InterPro; IPR007150; Hus1/Mec3.
DR Pfam; PF04005; Hus1; 1.
DR PIRSF; PIRSF011312; Cell_cycle_HUS1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; DNA damage; Nucleus; Reference proteome.
FT CHAIN 1..280
FT /note="Checkpoint protein HUS1"
FT /id="PRO_0000225004"
FT VAR_SEQ 119
FT /note="L -> LQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10395797,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9878245"
FT /id="VSP_017332"
FT VAR_SEQ 254..280
FT /note="NIVNNRTVHFDLLLEDVSLQYFIPALS -> SEFASPLSTSFVLHMQVCPVL
FT AIELPETVRLERSLEPEVSRDAEEE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017333"
SQ SEQUENCE 280 AA; 31680 MW; 8721B79853E6150D CRC64;
MKFRAKIVDL ACLNHFTRVS NMIAKLAKTC TLRISPEKLN FILCDKLASG GVSMWCELEQ
ENFFSEFQME GVSEENNEIY LELTSENLSR ALKTAQNSRA LKIKLTNKHF PCLTVSVELV
SSSSSSRIVV HDIPIKVLPR RLWKDLQEPS IPDCDVSICL PALKMMKSVV EKMRNISNQL
VIEANLKGEL NLKIETELVC VTTHFKDLEN PLLPSDSVSQ NRHPEDMAKV HIDIKKLLQF
LAGQQVTPTK AVCNIVNNRT VHFDLLLEDV SLQYFIPALS
