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Q9HAW4

- CLSPN_HUMAN

UniProt

Q9HAW4 - CLSPN_HUMAN

Protein

Claspin

Gene

CLSPN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
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    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.5 Publications

    GO - Molecular functioni

    1. anaphase-promoting complex binding Source: UniProtKB
    2. DNA binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of protein kinase activity Source: UniProtKB
    2. apoptotic process Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. DNA damage checkpoint Source: UniProtKB
    5. DNA repair Source: UniProtKB-KW
    6. DNA replication Source: Reactome
    7. G2 DNA damage checkpoint Source: UniProtKB
    8. mitotic DNA replication checkpoint Source: UniProtKB
    9. peptidyl-serine phosphorylation Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_6769. Activation of ATR in response to replication stress.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Claspin
    Short name:
    hClaspin
    Gene namesi
    Name:CLSPN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19715. CLSPN.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi916 – 9161T → A: Impairs interaction with CHEK1. 1 Publication
    Mutagenesisi945 – 9451S → A: Impairs interaction with CHEK1. 1 Publication
    Mutagenesisi982 – 9821S → A: No effect on interaction with CHEK1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134920757.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13391339ClaspinPRO_0000089875Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651Phosphoserine3 Publications
    Modified residuei67 – 671Phosphoserine3 Publications
    Modified residuei83 – 831Phosphoserine1 Publication
    Modified residuei225 – 2251Phosphoserine3 Publications
    Modified residuei718 – 7181Phosphoserine1 Publication
    Modified residuei720 – 7201Phosphoserine1 Publication
    Modified residuei723 – 7231Phosphoserine1 Publication
    Modified residuei808 – 8081Phosphoserine2 Publications
    Modified residuei810 – 8101Phosphoserine2 Publications
    Modified residuei833 – 8331Phosphoserine1 Publication
    Modified residuei839 – 8391Phosphoserine1 Publication
    Modified residuei846 – 8461Phosphoserine2 Publications
    Modified residuei891 – 8911N6-acetyllysine1 Publication
    Modified residuei916 – 9161Phosphothreonine; by CHEK11 Publication
    Modified residuei1012 – 10121Phosphoserine1 Publication
    Modified residuei1018 – 10181Phosphoserine1 Publication
    Modified residuei1020 – 10201Phosphoserine1 Publication
    Modified residuei1156 – 11561Phosphoserine2 Publications
    Modified residuei1289 – 12891Phosphoserine3 Publications

    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.9 Publications
    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.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9HAW4.
    PaxDbiQ9HAW4.
    PRIDEiQ9HAW4.

    PTM databases

    PhosphoSiteiQ9HAW4.

    Miscellaneous databases

    PMAP-CutDBQ2KHM3.

    Expressioni

    Inductioni

    Expression peaks at S/G2 phases of the cell cycle.1 Publication

    Gene expression databases

    ArrayExpressiQ9HAW4.
    BgeeiQ9HAW4.
    CleanExiHS_CLSPN.
    GenevestigatoriQ9HAW4.

    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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC45O754194EBI-1369377,EBI-374969
    CDK9P507503EBI-1369377,EBI-1383449
    CHEK1O147575EBI-1369377,EBI-974488
    FZR1Q9UM114EBI-1369377,EBI-724997

    Protein-protein interaction databases

    BioGridi122015. 24 interactions.
    IntActiQ9HAW4. 5 interactions.
    MINTiMINT-7897460.
    STRINGi9606.ENSP00000312995.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HAW4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati910 – 91910CKB motif 1
    Repeati939 – 94810CKB motif 2
    Repeati976 – 98510CKB motif 3

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili162 – 19635Sequence AnalysisAdd
    BLAST
    Coiled coili592 – 68190Sequence 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.

    Sequence similaritiesi

    Belongs to the claspin family.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG314362.
    HOVERGENiHBG080104.
    OMAiEEGNQET.
    OrthoDBiEOG77T13Q.
    PhylomeDBiQ9HAW4.
    TreeFamiTF328925.

    Family and domain databases

    InterProiIPR024146. Claspin.
    [Graphical view]
    PANTHERiPTHR14396. PTHR14396. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HAW4-1) [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

    MTGEVGSEVH LEINDPNVIS QEEADSPSDS GQGSYETIGP LSEGDSDEEI     50
    FVSKKLKNRK VLQDSDSETE DTNASPEKTT YDSAEEENKE NLYAGKNTKI 100
    KRIYKTVADS DESYMEKSLY QENLEAQVKP CLELSLQSGN STDFTTDRKS 150
    SKKHIHDKEG TAGKAKVKSK RRLEKEERKM EKIRQLKKKE TKNQEDDVEQ 200
    PFNDSGCLLV DKDLFETGLE DENNSPLEDE ESLESIRAAV KNKVKKHKKK 250
    EPSLESGVHS FEEGSELSKG TTRKERKAAR LSKEALKQLH SETQRLIRES 300
    ALNLPYHMPE NKTIHDFFKR KPRPTCHGNA MALLKSSKYQ SSHHKEIIDT 350
    ANTTEMNSDH HSKGSEQTTG AENEVETNAL PVVSKETQII TGSDESCRKD 400
    LVKNEELEIQ EKQKQSDIRP SPGDSSVLQQ ESNFLGNNHS EECQVGGLVA 450
    FEPHALEGEG PQNPEETDEK VEEPEQQNKS SAVGPPEKVR RFTLDRLKQL 500
    GVDVSIKPRL GADEDSFVIL EPETNRELEA LKQRFWKHAN PAAKPRAGQT 550
    VNVNVIVKDM GTDGKEELKA DVVPVTLAPK KLDGASHTKP GEKLQVLKAK 600
    LQEAMKLRRF EERQKRQALF KLDNEDGFEE EEEEEEEMTD ESEEDGEEKV 650
    EKEEKEEELE EEEEKEEEEE EEGNQETAEF LLSSEEIETK DEKEMDKENN 700
    DGSSEIGKAV GFLSVPKSLS SDSTLLLFKD SSSKMGYFPT EEKSETDENS 750
    GKQPSKLDED DSCSLLTKES SHNSSFELIG STIPSYQPCN RQTGRGTSFF 800
    PTAGGFRSPS PGLFRASLVS SASKSSGKLS EPSLPIEDSQ DLYNASPEPK 850
    TLFLGAGDFQ FCLEDDTQSQ LLDADGFLNV RNHRNQYQAL KPRLPLASMD 900
    ENAMDANMDE LLDLCTGKFT SQAEKHLPRK SDKKENMEEL LNLCSGKFTS 950
    QDASTPASSE LNKQEKESSM GDPMEEALAL CSGSFPTDKE EEDEEEEFGD 1000
    FRLVSNDNEF DSDEDEHSDS GNDLALEDHE DDDEEELLKR SEKLKRQMRL 1050
    RKYLEDEAEV SGSDVGSEDE YDGEEIDEYE EDVIDEVLPS DEELQSQIKK 1100
    IHMKTMLDDD KRQLRLYQER YLADGDLHSD GPGRMRKFRW KNIDDASQMD 1150
    LFHRDSDDDQ TEEQLDESEA RWRKERIERE QWLRDMAQQG KITAEEEEEI 1200
    GEDSQFMILA KKVTAKALQK NASRPMVIQE SKSLLRNPFE AIRPGSAQQV 1250
    KTGSLLNQPK AVLQKLAALS DHNPSAPRNS RNFVFHTLSP VKAEAAKESS 1300
    KSQVKKRGPS FMTSPSPKHL KTDDSTSGLT RSIFKYLES 1339
    Length:1,339
    Mass (Da):151,094
    Last modified:December 16, 2008 - v3
    Checksum:i3F3E392D5915955F
    GO
    Isoform 2 (identifier: Q9HAW4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         527-590: Missing.

    Show »
    Length:1,275
    Mass (Da):144,167
    Checksum:i5F02FE258D856D5C
    GO
    Isoform 3 (identifier: Q9HAW4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1304-1339: VKKRGPSFMTSPSPKHLKTDDSTSGLTRSIFKYLES → KIPEKDSDWLTWSGAPIPGFFRLSFDPHG

    Show »
    Length:1,332
    Mass (Da):150,368
    Checksum:i6FF64D7891BB7484
    GO

    Sequence cautioni

    The sequence AAH38991.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH62215.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341S → G in AAI15026. (PubMed:15489334)Curated
    Sequence conflicti446 – 4461G → E in AAI15026. (PubMed:15489334)Curated
    Sequence conflicti628 – 6281F → S in AAG24515. (PubMed:11090622)Curated
    Sequence conflicti664 – 6641E → G in AAG24515. (PubMed:11090622)Curated
    Sequence conflicti738 – 7381F → S in AAG24515. (PubMed:11090622)Curated
    Sequence conflicti931 – 9333SDK → GDE in AAI15026. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti439 – 4391H → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035674
    Natural varianti525 – 5251N → S.
    Corresponds to variant rs7537203 [ dbSNP | Ensembl ].
    VAR_023439
    Natural varianti892 – 8921P → T.
    Corresponds to variant rs34390044 [ dbSNP | Ensembl ].
    VAR_050867
    Natural varianti1280 – 12801S → L.
    Corresponds to variant rs35490896 [ dbSNP | Ensembl ].
    VAR_050868

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei527 – 59064Missing in isoform 2. 1 PublicationVSP_036033Add
    BLAST
    Alternative sequencei1304 – 133936VKKRG…KYLES → KIPEKDSDWLTWSGAPIPGF FRLSFDPHG in isoform 3. 1 PublicationVSP_036034Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF297866 mRNA. Translation: AAG24515.1.
    AL354864 Genomic DNA. Translation: CAH73807.2.
    BC038991 mRNA. Translation: AAH38991.1. Sequence problems.
    BC062215 mRNA. Translation: AAH62215.1. Sequence problems.
    BC113116 mRNA. Translation: AAI13117.1.
    BC115025 mRNA. Translation: AAI15026.1.
    BC137279 mRNA. Translation: AAI37280.1.
    BC140789 mRNA. Translation: AAI40790.1.
    CCDSiCCDS396.1. [Q9HAW4-1]
    CCDS53297.1. [Q9HAW4-2]
    RefSeqiNP_001177410.1. NM_001190481.1. [Q9HAW4-2]
    NP_071394.2. NM_022111.3. [Q9HAW4-1]
    UniGeneiHs.175613.

    Genome annotation databases

    EnsembliENST00000251195; ENSP00000251195; ENSG00000092853. [Q9HAW4-3]
    ENST00000318121; ENSP00000312995; ENSG00000092853. [Q9HAW4-1]
    ENST00000373220; ENSP00000362317; ENSG00000092853. [Q9HAW4-2]
    GeneIDi63967.
    KEGGihsa:63967.
    UCSCiuc001bzi.3. human. [Q9HAW4-1]
    uc009vux.3. human. [Q9HAW4-2]

    Polymorphism databases

    DMDMi218512100.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF297866 mRNA. Translation: AAG24515.1 .
    AL354864 Genomic DNA. Translation: CAH73807.2 .
    BC038991 mRNA. Translation: AAH38991.1 . Sequence problems.
    BC062215 mRNA. Translation: AAH62215.1 . Sequence problems.
    BC113116 mRNA. Translation: AAI13117.1 .
    BC115025 mRNA. Translation: AAI15026.1 .
    BC137279 mRNA. Translation: AAI37280.1 .
    BC140789 mRNA. Translation: AAI40790.1 .
    CCDSi CCDS396.1. [Q9HAW4-1 ]
    CCDS53297.1. [Q9HAW4-2 ]
    RefSeqi NP_001177410.1. NM_001190481.1. [Q9HAW4-2 ]
    NP_071394.2. NM_022111.3. [Q9HAW4-1 ]
    UniGenei Hs.175613.

    3D structure databases

    ProteinModelPortali Q9HAW4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122015. 24 interactions.
    IntActi Q9HAW4. 5 interactions.
    MINTi MINT-7897460.
    STRINGi 9606.ENSP00000312995.

    PTM databases

    PhosphoSitei Q9HAW4.

    Polymorphism databases

    DMDMi 218512100.

    Proteomic databases

    MaxQBi Q9HAW4.
    PaxDbi Q9HAW4.
    PRIDEi Q9HAW4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251195 ; ENSP00000251195 ; ENSG00000092853 . [Q9HAW4-3 ]
    ENST00000318121 ; ENSP00000312995 ; ENSG00000092853 . [Q9HAW4-1 ]
    ENST00000373220 ; ENSP00000362317 ; ENSG00000092853 . [Q9HAW4-2 ]
    GeneIDi 63967.
    KEGGi hsa:63967.
    UCSCi uc001bzi.3. human. [Q9HAW4-1 ]
    uc009vux.3. human. [Q9HAW4-2 ]

    Organism-specific databases

    CTDi 63967.
    GeneCardsi GC01M036185.
    HGNCi HGNC:19715. CLSPN.
    MIMi 605434. gene.
    neXtProti NX_Q9HAW4.
    PharmGKBi PA134920757.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314362.
    HOVERGENi HBG080104.
    OMAi EEGNQET.
    OrthoDBi EOG77T13Q.
    PhylomeDBi Q9HAW4.
    TreeFami TF328925.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_6769. Activation of ATR in response to replication stress.

    Miscellaneous databases

    GeneWikii CLSPN.
    GenomeRNAii 63967.
    NextBioi 65748.
    PMAP-CutDB Q2KHM3.
    PROi Q9HAW4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAW4.
    Bgeei Q9HAW4.
    CleanExi HS_CLSPN.
    Genevestigatori Q9HAW4.

    Family and domain databases

    InterProi IPR024146. Claspin.
    [Graphical view ]
    PANTHERi PTHR14396. PTHR14396. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Claspin, a novel protein required for the activation of Chk1 during a DNA replication checkpoint response in Xenopus egg extracts."
      Kumagai A., Dunphy W.G.
      Mol. Cell 6:839-849(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Skin.
    4. "Human claspin is required for replication checkpoint control."
      Chini C.C.S., Chen J.
      J. Biol. Chem. 278:30057-30062(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHEK1; ATR AND RAD9A, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION.
    5. "ATR, claspin and the Rad9-Rad1-Hus1 complex regulate Chk1 and Cdc25A in the absence of DNA damage."
      Sorensen C.S., Syljuasen R.G., Lukas J., Bartek J.
      Cell Cycle 3:941-945(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Human claspin is a ring-shaped DNA-binding protein with high affinity to branched DNA structures."
      Sar F., Lindsey-Boltz L.A., Subramanian D., Croteau D.L., Hutsell S.Q., Griffith J.D., Sancar A.
      J. Biol. Chem. 279:39289-39295(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Human claspin works with BRCA1 to both positively and negatively regulate cell proliferation."
      Lin S.-Y., Li K., Stewart G.S., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION BY ATR.
    8. "DNA-dependent phosphorylation of Chk1 and claspin in a human cell-free system."
      Clarke C.A.L., Clarke P.R.
      Biochem. J. 388:705-712(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHEK1, MUTAGENESIS OF THR-916; SER-945 AND SER-982.
    9. "A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response."
      Zhang D., Zaugg K., Mak T.W., Elledge S.J.
      Cell 126:529-542(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Repeated phosphopeptide motifs in human Claspin are phosphorylated by Chk1 and mediate Claspin function."
      Chini C.C., Chen J.
      J. Biol. Chem. 281:33276-33282(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-916 BY CHEK1, INTERACTION WITH CHEK1.
    12. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
      Gotter A.L., Suppa C., Emanuel B.S.
      J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIMELESS.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. "The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint."
      Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M.
      Cell 134:256-267(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY THE APC/C COMPLEX, DEUBIQUITINATION BY USP28, INTERACTION WITH FZR1.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-67; SER-225; SER-720; SER-808; SER-810; SER-846; SER-1012; SER-1018; SER-1020; SER-1156 AND SER-1289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839; SER-846; SER-1156 AND SER-1289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-891, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-67; SER-225; SER-718; SER-723; SER-808; SER-810 AND SER-1289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1."
      Meng Z., Capalbo L., Glover D.M., Dunphy W.G.
      Mol. Biol. Cell 22:2834-2847(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSNK1G1/CK1.
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-67; SER-83 AND SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-439.

    Entry informationi

    Entry nameiCLSPN_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAW4
    Secondary accession number(s): A6NFL4
    , Q1RMC6, Q2KHM3, Q5VYG0, Q6P6H5, Q8IWI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3