Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8BQY8

- HUS1_MOUSE

UniProt

Q8BQY8 - HUS1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Checkpoint protein HUS1

Gene

Hus1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. cellular response to ionizing radiation Source: Ensembl
  3. DNA damage checkpoint Source: MGI
  4. double-strand break repair via homologous recombination Source: UniProtKB
  5. embryo development Source: UniProtKB
  6. mitotic cell cycle checkpoint Source: UniProtKB
  7. negative regulation of DNA replication Source: UniProtKB
  8. protein phosphorylation Source: MGI
  9. regulation of protein phosphorylation Source: UniProtKB
  10. response to UV Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage

Enzyme and pathway databases

ReactomeiREACT_232236. Activation of ATR in response to replication stress.

Names & Taxonomyi

Protein namesi
Recommended name:
Checkpoint protein HUS1
Short name:
mHUS1
Gene namesi
Name:Hus1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1277962. Hus1.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity
Note: In discrete nuclear foci upon DNA damage. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm (By similarity).By similarity

GO - Cellular componenti

  1. checkpoint clamp complex Source: InterPro
  2. cytoplasm Source: UniProtKB-KW
  3. nucleolus Source: InterPro
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Checkpoint protein HUS1PRO_0000225004Add
BLAST

Proteomic databases

MaxQBiQ8BQY8.
PRIDEiQ8BQY8.

PTM databases

PhosphoSiteiQ8BQY8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8BQY8.
CleanExiMM_HUS1.
GenevestigatoriQ8BQY8.

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BQY8.
SMRiQ8BQY8. Positions 3-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HUS1 family.Curated

Phylogenomic databases

eggNOGiNOG250864.
GeneTreeiENSGT00390000000706.
HOGENOMiHOG000253011.
HOVERGENiHBG053069.
InParanoidiQ8BQY8.
KOiK10903.
OMAiCMILYVY.
OrthoDBiEOG780RN2.
PhylomeDBiQ8BQY8.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BQY8-1) [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
MKFRAKIVDL ACLNHFTRVS NMIAKLAKTC TLRISPEKLN FILCDKLASG
60 70 80 90 100
GVSMWCELEQ ENFFSEFQME GVSEENNEIY LELTSENLSR ALKTAQNSRA
110 120 130 140 150
LKIKLTNKHF PCLTVSVELV SSSSSSRIVV HDIPIKVLPR RLWKDLQEPS
160 170 180 190 200
IPDCDVSICL PALKMMKSVV EKMRNISNQL VIEANLKGEL NLKIETELVC
210 220 230 240 250
VTTHFKDLEN PLLPSDSVSQ NRHPEDMAKV HIDIKKLLQF LAGQQVTPTK
260 270 280
AVCNIVNNRT VHFDLLLEDV SLQYFIPALS
Length:280
Mass (Da):31,680
Last modified:March 1, 2003 - v1
Checksum:i8721B79853E6150D
GO
Isoform 2 (identifier: Q8BQY8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: L → LQ

Show »
Length:281
Mass (Da):31,808
Checksum:iE34F90D989912285
GO
Isoform 3 (identifier: Q8BQY8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: L → LQ
     254-280: NIVNNRTVHFDLLLEDVSLQYFIPALS → SEFASPLSTSFVLHMQVCPVLAIELPETVRLERSLEPEVSRDAEEE

Note: No experimental confirmation available.

Show »
Length:300
Mass (Da):33,848
Checksum:i947D0A24ECE9CB71
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei119 – 1191L → LQ in isoform 2 and isoform 3. 4 PublicationsVSP_017332
Alternative sequencei254 – 28027NIVNN…IPALS → SEFASPLSTSFVLHMQVCPV LAIELPETVRLERSLEPEVS RDAEEE in isoform 3. 1 PublicationVSP_017333Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16894 mRNA. Translation: CAA76519.1.
AF076845 mRNA. Translation: AAC95527.1.
AK046152 mRNA. Translation: BAC32614.1.
AK088403 mRNA. Translation: BAC40332.1.
AK135922 mRNA. Translation: BAE22725.1.
AL669837 Genomic DNA. Translation: CAI24619.1.
BC061249 mRNA. Translation: AAH61249.1.
CCDSiCCDS24429.1. [Q8BQY8-2]
RefSeqiNP_032342.1. NM_008316.4. [Q8BQY8-2]
XP_006514594.1. XM_006514531.1. [Q8BQY8-3]
XP_006514595.1. XM_006514532.1. [Q8BQY8-1]
UniGeneiMm.42201.

Genome annotation databases

EnsembliENSMUST00000020683; ENSMUSP00000020683; ENSMUSG00000020413. [Q8BQY8-2]
ENSMUST00000129115; ENSMUSP00000114339; ENSMUSG00000020413. [Q8BQY8-2]
GeneIDi15574.
KEGGimmu:15574.
UCSCiuc007hzp.1. mouse. [Q8BQY8-1]
uc007hzq.1. mouse. [Q8BQY8-2]
uc007hzs.1. mouse. [Q8BQY8-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16894 mRNA. Translation: CAA76519.1 .
AF076845 mRNA. Translation: AAC95527.1 .
AK046152 mRNA. Translation: BAC32614.1 .
AK088403 mRNA. Translation: BAC40332.1 .
AK135922 mRNA. Translation: BAE22725.1 .
AL669837 Genomic DNA. Translation: CAI24619.1 .
BC061249 mRNA. Translation: AAH61249.1 .
CCDSi CCDS24429.1. [Q8BQY8-2 ]
RefSeqi NP_032342.1. NM_008316.4. [Q8BQY8-2 ]
XP_006514594.1. XM_006514531.1. [Q8BQY8-3 ]
XP_006514595.1. XM_006514532.1. [Q8BQY8-1 ]
UniGenei Mm.42201.

3D structure databases

ProteinModelPortali Q8BQY8.
SMRi Q8BQY8. Positions 3-280.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BQY8.

Proteomic databases

MaxQBi Q8BQY8.
PRIDEi Q8BQY8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020683 ; ENSMUSP00000020683 ; ENSMUSG00000020413 . [Q8BQY8-2 ]
ENSMUST00000129115 ; ENSMUSP00000114339 ; ENSMUSG00000020413 . [Q8BQY8-2 ]
GeneIDi 15574.
KEGGi mmu:15574.
UCSCi uc007hzp.1. mouse. [Q8BQY8-1 ]
uc007hzq.1. mouse. [Q8BQY8-2 ]
uc007hzs.1. mouse. [Q8BQY8-3 ]

Organism-specific databases

CTDi 3364.
MGIi MGI:1277962. Hus1.

Phylogenomic databases

eggNOGi NOG250864.
GeneTreei ENSGT00390000000706.
HOGENOMi HOG000253011.
HOVERGENi HBG053069.
InParanoidi Q8BQY8.
KOi K10903.
OMAi CMILYVY.
OrthoDBi EOG780RN2.
PhylomeDBi Q8BQY8.
TreeFami TF314491.

Enzyme and pathway databases

Reactomei REACT_232236. Activation of ATR in response to replication stress.

Miscellaneous databases

NextBioi 288568.
PROi Q8BQY8.
SOURCEi Search...

Gene expression databases

Bgeei Q8BQY8.
CleanExi MM_HUS1.
Genevestigatori Q8BQY8.

Family and domain databases

InterProi IPR016580. Cell_cycle_HUS1.
IPR007150. Hus1/Mec3.
[Graphical view ]
PANTHERi PTHR12900. PTHR12900. 1 hit.
Pfami PF04005. Hus1. 1 hit.
[Graphical view ]
PIRSFi PIRSF011312. Cell_cycle_HUS1. 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. "Mouse Hus1, a homologue of the Schizosaccharomyces pombe hus1+ cell cycle checkpoint gene."
    Weiss R.S., Kostrub C.F., Enoch T., Leder P.
    Genomics 59:32-39(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Corpora quadrigemina, Egg and Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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 3).
    Tissue: Pituitary.

Entry informationi

Entry nameiHUS1_MOUSE
AccessioniPrimary (citable) accession number: Q8BQY8
Secondary accession number(s): O70543, Q6P8H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3