CLSPN_MOUSE
ID CLSPN_MOUSE Reviewed; 1315 AA.
AC Q80YR7; B1ARX6; Q69GM2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Claspin;
GN Name=Clspn;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 906-1315.
RC STRAIN=ICR; TISSUE=Testis;
RA Hasthorpe S.;
RT "Checkpoint control in gametogenesis.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-42; SER-46; SER-53;
RP SER-65; SER-67; SER-109; SER-112; SER-119; SER-816; SER-823; SER-1133 AND
RP SER-1265, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for checkpoint mediated cell cycle arrest in
CC response to inhibition of DNA replication or to DNA damage induced by
CC both ionizing and UV irradiation. Adapter protein which binds to BRCA1
CC and the checkpoint kinase CHEK1 and facilitates the ATR-dependent
CC phosphorylation of both proteins. Can also bind specifically to
CC branched DNA structures and may associate with S-phase chromatin
CC following formation of the pre-replication complex (pre-RC). This may
CC indicate a role for this protein as a sensor which monitors the
CC integrity of DNA replication forks (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (phosphorylation-dependent) with CHEK1; regulates
CC CLSPN function in checkpoint for DNA damage and replication. Interacts
CC with ATR and RAD9A and these interactions are slightly reduced during
CC checkpoint activation. Interacts with BRCA1 and this interaction
CC increases during checkpoint activation. Interacts with TIMELESS (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: The C-terminus of the protein contains 3 potential CHEK1-
CC binding motifs (CKB motifs). Potential phosphorylation sites within CKB
CC motif 1 and CKB motif 2 are required for interaction with CHEK1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Undergoes ATR-dependent phosphorylation by CHEK1
CC during activation of DNA replication or damage checkpoints.
CC Phosphorylation by CSNK1G1/CK1 promotes CHEK1 binding (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C)
CC during G1 phase, leading to its degradation by the proteasome.
CC Ubiquitination is mediated via its interaction with FZR1/CDH1.
CC Following DNA damage, it is deubiquitinated by USP28 in G2 phase,
CC preventing its degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the claspin family. {ECO:0000305}.
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DR EMBL; AL606935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050848; AAH50848.1; -; mRNA.
DR EMBL; AY324187; AAP97538.1; -; mRNA.
DR CCDS; CCDS18655.1; -.
DR RefSeq; NP_780763.3; NM_175554.4.
DR RefSeq; XP_011238843.1; XM_011240541.2.
DR AlphaFoldDB; Q80YR7; -.
DR SMR; Q80YR7; -.
DR BioGRID; 234671; 23.
DR IntAct; Q80YR7; 16.
DR STRING; 10090.ENSMUSP00000045344; -.
DR iPTMnet; Q80YR7; -.
DR PhosphoSitePlus; Q80YR7; -.
DR EPD; Q80YR7; -.
DR jPOST; Q80YR7; -.
DR MaxQB; Q80YR7; -.
DR PaxDb; Q80YR7; -.
DR PeptideAtlas; Q80YR7; -.
DR PRIDE; Q80YR7; -.
DR ProteomicsDB; 285495; -.
DR Antibodypedia; 17335; 107 antibodies from 30 providers.
DR DNASU; 269582; -.
DR Ensembl; ENSMUST00000048391; ENSMUSP00000045344; ENSMUSG00000042489.
DR GeneID; 269582; -.
DR KEGG; mmu:269582; -.
DR UCSC; uc008utm.2; mouse.
DR CTD; 63967; -.
DR MGI; MGI:2445153; Clspn.
DR VEuPathDB; HostDB:ENSMUSG00000042489; -.
DR eggNOG; KOG4156; Eukaryota.
DR GeneTree; ENSGT00390000012738; -.
DR HOGENOM; CLU_005892_0_0_1; -.
DR InParanoid; Q80YR7; -.
DR OMA; TEMNGDH; -.
DR OrthoDB; 132723at2759; -.
DR TreeFam; TF328925; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR BioGRID-ORCS; 269582; 12 hits in 110 CRISPR screens.
DR ChiTaRS; Clspn; mouse.
DR PRO; PR:Q80YR7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80YR7; protein.
DR Bgee; ENSMUSG00000042489; Expressed in embryonic post-anal tail and 152 other tissues.
DR ExpressionAtlas; Q80YR7; baseline and differential.
DR Genevisible; Q80YR7; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0010997; F:anaphase-promoting complex binding; ISO:MGI.
DR GO; GO:0000217; F:DNA secondary structure binding; ISO:MGI.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; ISO:MGI.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; ISO:MGI.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR InterPro; IPR024146; Claspin.
DR PANTHER; PTHR14396; PTHR14396; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Chromosome; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1315
FT /note="Claspin"
FT /id="PRO_0000089876"
FT REPEAT 887..896
FT /note="CKB motif 1"
FT REPEAT 917..926
FT /note="CKB motif 2"
FT REPEAT 954..963
FT /note="CKB motif 3"
FT REGION 22..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 159..187
FT /evidence="ECO:0000255"
FT COILED 599..626
FT /evidence="ECO:0000255"
FT COILED 1001..1036
FT /evidence="ECO:0000255"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..661
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 868
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 893
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW4"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 727
FT /note="Y -> H (in Ref. 2; AAH50848)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="E -> EE (in Ref. 3; AAP97538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1315 AA; 146715 MW; 762AA39E19D8EAA3 CRC64;
MTGEVGSEVN LEVNDLKLLS QEAADSPVDS GQGSFETLEP LSERDSDEEI FVSKKPKSRK
VLQDSDSEAE DRDDAPEKPT YDDSAEDTQE NLHSGKSQSR SFPKALADSD ESDMEETPSQ
ESPETQEAPS LEPGHQTGHS VDFTTGRKLS KTLLREGAEG KAKSKRRLEK EERTMEKIRR
LKKKETRCEE SDADRPLNDS GCLLEDSDLF ETGLEEENDS ALEDEESLES IRAAVKNKVK
NRKKKEPTLE SEAFSLEDGN ELSKGSARKE RKAARLSKEA LKKLHSETQR LVRESALNLP
YHMPESKTIH DFFKRKPRPT CQGSAMALLK SCKYQSGHYK ETVNPADAAG MGAEDSSRGS
EQRTGAGIAA ETNVLSEVSE EAGITAGSDE ACGKDPVRRG ELEIEETEKH SDDRPYSPGD
RSMSQQESSI PRIEDNEGHQ AGDLTESDPP ALEGEELKTV EKTDAKEGMP EQKTQSAAAA
AVAVVTAAAA PPEKVRRFTV DRLRQLGVDV SSQPRLGADE DSFVILDEPK TNRELEALKQ
RFWRHANPAA SPRACQTVNV NIIVKDLGTN GKEELKAEVV PVTLAAEKLE GASHAKPGEK
LQMLKAKLQE AMKLRRLEER QKRQALFKLD NEDGFEEEEE EEEMTDESEE DGEEETTEYL
LGSEDTETKD EKETDKENTD TSSDIGKSVA LCVPKPLSSD STLLLFKDSS SKMGYFPTEE
KSETDEYLAK QSDKLDEDDS SSLLTKESSH NSSFELIGST IPSYQPCNRQ IGRGASFLPT
AGFRSPSPGL FRGSLISSAS KSSGKLSEPS LPVEDSQDLY TASPEPKTLF LGAGDFQFCL
EDDTQSQLLD ADGFLNIRNH RHRYQAVKPQ LPLASMDENA MDANMDELLD LCTGQFTSQP
EEKCQPRKND KKENMEELLN LCSGKFPTQD ASPVAPLGLR SQEKESSTED PMEEALALCS
GSFPTDREEE GEEEEFGDFQ LVSKENGFAS DEDEHSDSND EELALDLEDD EEELLKQSEK
MKRQMRLKKY LEDEAEVSGS DVGSEDEYDG EEIDEYEEDV IDEVLPSDEE LESQIKKIHM
KTMLDDDKRR LRLYQERYLA DGDLHSDGPG RTRKFRWKHI DDTSQMDLFH RDSDDDQVEE
QLDETEAKWR KERIEREQWL REQAQQGKIA ADEEDIGDDS QFMMLAKKVT AKALQKNASH
TVVVQESKSV LRNPFETIRP GGAHQLKTGS LLNQPKAVLQ KLAALSDLNP SAPRNSRNFV
FHTLSPTKAE AAKDSSKPQV RRRGLSSMMS PSPKRLKTNG SSPGPKRSIF RYLES
