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Q9HAW4

- CLSPN_HUMAN

UniProt

Q9HAW4 - CLSPN_HUMAN

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Protein

Claspin

Gene
CLSPN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.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
Complete GO annotation...

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
Complete GO annotation...

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.4 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.

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 – 19635 Reviewed predictionAdd
BLAST
Coiled coili592 – 68190 Reviewed predictionAdd
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.

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.

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. VSP_036033Add
BLAST
Alternative sequencei1304 – 133936VKKRG…KYLES → KIPEKDSDWLTWSGAPIPGF FRLSFDPHG in isoform 3. VSP_036034Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → G in AAI15026. 1 Publication
Sequence conflicti446 – 4461G → E in AAI15026. 1 Publication
Sequence conflicti628 – 6281F → S in AAG24515. 1 Publication
Sequence conflicti664 – 6641E → G in AAG24515. 1 Publication
Sequence conflicti738 – 7381F → S in AAG24515. 1 Publication
Sequence conflicti931 – 9333SDK → GDE in AAI15026. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 106 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

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