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Protein

Claspin

Gene

Clspn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation. Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins. Can also bind specifically to branched DNA structures and may associate with S-phase chromatin following formation of the pre-replication complex (pre-RC). This may indicate a role for this protein as a sensor which monitors the integrity of DNA replication forks (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-5693607. Processing of DNA double-strand break ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Claspin
Gene namesi
Name:Clspn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2445153. Clspn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13151315ClaspinPRO_0000089876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei42 – 421PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei65 – 651PhosphoserineCombined sources
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei109 – 1091PhosphoserineCombined sources
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei119 – 1191PhosphoserineCombined sources
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei698 – 6981PhosphoserineBy similarity
Modified residuei701 – 7011PhosphoserineBy similarity
Modified residuei709 – 7091PhosphoserineBy similarity
Modified residuei722 – 7221PhosphoserineBy similarity
Modified residuei740 – 7401PhosphoserineBy similarity
Modified residuei785 – 7851PhosphoserineBy similarity
Modified residuei787 – 7871PhosphoserineBy similarity
Modified residuei810 – 8101PhosphoserineBy similarity
Modified residuei816 – 8161PhosphoserineCombined sources
Modified residuei823 – 8231PhosphoserineCombined sources
Modified residuei868 – 8681N6-acetyllysineBy similarity
Modified residuei893 – 8931Phosphothreonine; by CHEK1By similarity
Modified residuei932 – 9321PhosphoserineBy similarity
Modified residuei990 – 9901PhosphoserineBy similarity
Modified residuei996 – 9961PhosphoserineBy similarity
Modified residuei998 – 9981PhosphoserineBy similarity
Modified residuei1133 – 11331PhosphoserineCombined sources
Modified residuei1265 – 12651PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Undergoes ATR-dependent phosphorylation by CHEK1 during activation of DNA replication or damage checkpoints. Phosphorylation by CSNK1G1/CK1 promotes CHEK1 binding (By similarity).By similarity
Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) during G1 phase, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Following DNA damage, it is deubiquitinated by USP28 in G2 phase, preventing its degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ80YR7.
MaxQBiQ80YR7.
PaxDbiQ80YR7.
PeptideAtlasiQ80YR7.
PRIDEiQ80YR7.

PTM databases

iPTMnetiQ80YR7.
PhosphoSiteiQ80YR7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000042489.
CleanExiMM_CLSPN.
ExpressionAtlasiQ80YR7. baseline and differential.
GenevisibleiQ80YR7. MM.

Interactioni

Subunit structurei

Interacts (phosphorylation-dependent) with CHEK1; regulates CLSPN function in checkpoint for DNA damage and replication. Interacts with ATR and RAD9A and these interactions are slightly reduced during checkpoint activation. Interacts with BRCA1 and this interaction increases during checkpoint activation. Interacts with TIMELESS (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi234671. 17 interactions.
IntActiQ80YR7. 16 interactions.
STRINGi10090.ENSMUSP00000045344.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati887 – 89610CKB motif 1
Repeati917 – 92610CKB motif 2
Repeati954 – 96310CKB motif 3

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili159 – 18729Sequence analysisAdd
BLAST
Coiled coili599 – 62628Sequence analysisAdd
BLAST
Coiled coili1001 – 103636Sequence analysisAdd
BLAST

Domaini

The C-terminus of the protein contains 3 potential CHEK1-binding motifs (CKB motifs). Potential phosphorylation sites within CKB motif 1 and CKB motif 2 are required for interaction with CHEK1 (By similarity).By similarity

Sequence similaritiesi

Belongs to the claspin family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG4156. Eukaryota.
ENOG410Y041. LUCA.
GeneTreeiENSGT00390000012738.
HOGENOMiHOG000049140.
HOVERGENiHBG080104.
InParanoidiQ80YR7.
OMAiIRAAMKN.
OrthoDBiEOG091G0CRX.
TreeFamiTF328925.

Family and domain databases

InterProiIPR024146. Claspin.
[Graphical view]
PANTHERiPTHR14396. PTHR14396. 2 hits.

Sequencei

Sequence statusi: Complete.

Q80YR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGEVGSEVN LEVNDLKLLS QEAADSPVDS GQGSFETLEP LSERDSDEEI
60 70 80 90 100
FVSKKPKSRK VLQDSDSEAE DRDDAPEKPT YDDSAEDTQE NLHSGKSQSR
110 120 130 140 150
SFPKALADSD ESDMEETPSQ ESPETQEAPS LEPGHQTGHS VDFTTGRKLS
160 170 180 190 200
KTLLREGAEG KAKSKRRLEK EERTMEKIRR LKKKETRCEE SDADRPLNDS
210 220 230 240 250
GCLLEDSDLF ETGLEEENDS ALEDEESLES IRAAVKNKVK NRKKKEPTLE
260 270 280 290 300
SEAFSLEDGN ELSKGSARKE RKAARLSKEA LKKLHSETQR LVRESALNLP
310 320 330 340 350
YHMPESKTIH DFFKRKPRPT CQGSAMALLK SCKYQSGHYK ETVNPADAAG
360 370 380 390 400
MGAEDSSRGS EQRTGAGIAA ETNVLSEVSE EAGITAGSDE ACGKDPVRRG
410 420 430 440 450
ELEIEETEKH SDDRPYSPGD RSMSQQESSI PRIEDNEGHQ AGDLTESDPP
460 470 480 490 500
ALEGEELKTV EKTDAKEGMP EQKTQSAAAA AVAVVTAAAA PPEKVRRFTV
510 520 530 540 550
DRLRQLGVDV SSQPRLGADE DSFVILDEPK TNRELEALKQ RFWRHANPAA
560 570 580 590 600
SPRACQTVNV NIIVKDLGTN GKEELKAEVV PVTLAAEKLE GASHAKPGEK
610 620 630 640 650
LQMLKAKLQE AMKLRRLEER QKRQALFKLD NEDGFEEEEE EEEMTDESEE
660 670 680 690 700
DGEEETTEYL LGSEDTETKD EKETDKENTD TSSDIGKSVA LCVPKPLSSD
710 720 730 740 750
STLLLFKDSS SKMGYFPTEE KSETDEYLAK QSDKLDEDDS SSLLTKESSH
760 770 780 790 800
NSSFELIGST IPSYQPCNRQ IGRGASFLPT AGFRSPSPGL FRGSLISSAS
810 820 830 840 850
KSSGKLSEPS LPVEDSQDLY TASPEPKTLF LGAGDFQFCL EDDTQSQLLD
860 870 880 890 900
ADGFLNIRNH RHRYQAVKPQ LPLASMDENA MDANMDELLD LCTGQFTSQP
910 920 930 940 950
EEKCQPRKND KKENMEELLN LCSGKFPTQD ASPVAPLGLR SQEKESSTED
960 970 980 990 1000
PMEEALALCS GSFPTDREEE GEEEEFGDFQ LVSKENGFAS DEDEHSDSND
1010 1020 1030 1040 1050
EELALDLEDD EEELLKQSEK MKRQMRLKKY LEDEAEVSGS DVGSEDEYDG
1060 1070 1080 1090 1100
EEIDEYEEDV IDEVLPSDEE LESQIKKIHM KTMLDDDKRR LRLYQERYLA
1110 1120 1130 1140 1150
DGDLHSDGPG RTRKFRWKHI DDTSQMDLFH RDSDDDQVEE QLDETEAKWR
1160 1170 1180 1190 1200
KERIEREQWL REQAQQGKIA ADEEDIGDDS QFMMLAKKVT AKALQKNASH
1210 1220 1230 1240 1250
TVVVQESKSV LRNPFETIRP GGAHQLKTGS LLNQPKAVLQ KLAALSDLNP
1260 1270 1280 1290 1300
SAPRNSRNFV FHTLSPTKAE AAKDSSKPQV RRRGLSSMMS PSPKRLKTNG
1310
SSPGPKRSIF RYLES
Length:1,315
Mass (Da):146,715
Last modified:July 27, 2011 - v2
Checksum:i762AA39E19D8EAA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti727 – 7271Y → H in AAH50848 (PubMed:15489334).Curated
Sequence conflicti1013 – 10131E → EE in AAP97538 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL606935 Genomic DNA. Translation: CAM17430.1.
BC050848 mRNA. Translation: AAH50848.1.
AY324187 mRNA. Translation: AAP97538.1.
CCDSiCCDS18655.1.
RefSeqiNP_780763.3. NM_175554.4.
XP_011238843.1. XM_011240541.1.
UniGeneiMm.243962.

Genome annotation databases

EnsembliENSMUST00000048391; ENSMUSP00000045344; ENSMUSG00000042489.
GeneIDi269582.
KEGGimmu:269582.
UCSCiuc008utm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL606935 Genomic DNA. Translation: CAM17430.1.
BC050848 mRNA. Translation: AAH50848.1.
AY324187 mRNA. Translation: AAP97538.1.
CCDSiCCDS18655.1.
RefSeqiNP_780763.3. NM_175554.4.
XP_011238843.1. XM_011240541.1.
UniGeneiMm.243962.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234671. 17 interactions.
IntActiQ80YR7. 16 interactions.
STRINGi10090.ENSMUSP00000045344.

PTM databases

iPTMnetiQ80YR7.
PhosphoSiteiQ80YR7.

Proteomic databases

EPDiQ80YR7.
MaxQBiQ80YR7.
PaxDbiQ80YR7.
PeptideAtlasiQ80YR7.
PRIDEiQ80YR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048391; ENSMUSP00000045344; ENSMUSG00000042489.
GeneIDi269582.
KEGGimmu:269582.
UCSCiuc008utm.2. mouse.

Organism-specific databases

CTDi63967.
MGIiMGI:2445153. Clspn.

Phylogenomic databases

eggNOGiKOG4156. Eukaryota.
ENOG410Y041. LUCA.
GeneTreeiENSGT00390000012738.
HOGENOMiHOG000049140.
HOVERGENiHBG080104.
InParanoidiQ80YR7.
OMAiIRAAMKN.
OrthoDBiEOG091G0CRX.
TreeFamiTF328925.

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-5693607. Processing of DNA double-strand break ends.

Miscellaneous databases

ChiTaRSiClspn. mouse.
PROiQ80YR7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000042489.
CleanExiMM_CLSPN.
ExpressionAtlasiQ80YR7. baseline and differential.
GenevisibleiQ80YR7. MM.

Family and domain databases

InterProiIPR024146. Claspin.
[Graphical view]
PANTHERiPTHR14396. PTHR14396. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCLSPN_MOUSE
AccessioniPrimary (citable) accession number: Q80YR7
Secondary accession number(s): B1ARX6, Q69GM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 95 of the entry and version 2 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

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 one 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.