CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021589
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Claspin 
Protein Synonyms/Alias
 hClaspin 
Gene Name
 CLSPN 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
105TKIKRIYKTVADSDEubiquitination[1]
412EELEIQEKQKQSDIRubiquitination[1]
414LEIQEKQKQSDIRPSubiquitination[1]
507LGVDVSIKPRLGADEubiquitination[1]
734LFKDSSSKMGYFPTEubiquitination[2]
891RNQYQALKPRLPLASacetylation[3]
891RNQYQALKPRLPLASubiquitination[1]
925KFTSQAEKHLPRKSDacetylation[3]
963PASSELNKQEKESSMubiquitination[2]
1265QPKAVLQKLAALSDHubiquitination[1]
1321SPSPKHLKTDDSTSGubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 910 919 CKB motif 1.
 REPEAT 939 948 CKB motif 2.
 REPEAT 976 985 CKB motif 3.
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 225 225 Phosphoserine.
 MOD_RES 718 718 Phosphoserine.
 MOD_RES 720 720 Phosphoserine.
 MOD_RES 723 723 Phosphoserine.
 MOD_RES 808 808 Phosphoserine.
 MOD_RES 810 810 Phosphoserine.
 MOD_RES 833 833 Phosphoserine.
 MOD_RES 839 839 Phosphoserine.
 MOD_RES 846 846 Phosphoserine.
 MOD_RES 891 891 N6-acetyllysine.
 MOD_RES 916 916 Phosphothreonine; by CHEK1.
 MOD_RES 1012 1012 Phosphoserine.
 MOD_RES 1018 1018 Phosphoserine.
 MOD_RES 1020 1020 Phosphoserine.
 MOD_RES 1156 1156 Phosphoserine.
 MOD_RES 1289 1289 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Coiled coil; Complete proteome; DNA damage; DNA repair; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1339 AA 
Protein Sequence
MTGEVGSEVH LEINDPNVIS QEEADSPSDS GQGSYETIGP LSEGDSDEEI FVSKKLKNRK 60
VLQDSDSETE DTNASPEKTT YDSAEEENKE NLYAGKNTKI KRIYKTVADS DESYMEKSLY 120
QENLEAQVKP CLELSLQSGN STDFTTDRKS SKKHIHDKEG TAGKAKVKSK RRLEKEERKM 180
EKIRQLKKKE TKNQEDDVEQ PFNDSGCLLV DKDLFETGLE DENNSPLEDE ESLESIRAAV 240
KNKVKKHKKK EPSLESGVHS FEEGSELSKG TTRKERKAAR LSKEALKQLH SETQRLIRES 300
ALNLPYHMPE NKTIHDFFKR KPRPTCHGNA MALLKSSKYQ SSHHKEIIDT ANTTEMNSDH 360
HSKGSEQTTG AENEVETNAL PVVSKETQII TGSDESCRKD LVKNEELEIQ EKQKQSDIRP 420
SPGDSSVLQQ ESNFLGNNHS EECQVGGLVA FEPHALEGEG PQNPEETDEK VEEPEQQNKS 480
SAVGPPEKVR RFTLDRLKQL GVDVSIKPRL GADEDSFVIL EPETNRELEA LKQRFWKHAN 540
PAAKPRAGQT VNVNVIVKDM GTDGKEELKA DVVPVTLAPK KLDGASHTKP GEKLQVLKAK 600
LQEAMKLRRF EERQKRQALF KLDNEDGFEE EEEEEEEMTD ESEEDGEEKV EKEEKEEELE 660
EEEEKEEEEE EEGNQETAEF LLSSEEIETK DEKEMDKENN DGSSEIGKAV GFLSVPKSLS 720
SDSTLLLFKD SSSKMGYFPT EEKSETDENS GKQPSKLDED DSCSLLTKES SHNSSFELIG 780
STIPSYQPCN RQTGRGTSFF PTAGGFRSPS PGLFRASLVS SASKSSGKLS EPSLPIEDSQ 840
DLYNASPEPK TLFLGAGDFQ FCLEDDTQSQ LLDADGFLNV RNHRNQYQAL KPRLPLASMD 900
ENAMDANMDE LLDLCTGKFT SQAEKHLPRK SDKKENMEEL LNLCSGKFTS QDASTPASSE 960
LNKQEKESSM GDPMEEALAL CSGSFPTDKE EEDEEEEFGD FRLVSNDNEF DSDEDEHSDS 1020
GNDLALEDHE DDDEEELLKR SEKLKRQMRL RKYLEDEAEV SGSDVGSEDE YDGEEIDEYE 1080
EDVIDEVLPS DEELQSQIKK IHMKTMLDDD KRQLRLYQER YLADGDLHSD GPGRMRKFRW 1140
KNIDDASQMD LFHRDSDDDQ TEEQLDESEA RWRKERIERE QWLRDMAQQG KITAEEEEEI 1200
GEDSQFMILA KKVTAKALQK NASRPMVIQE SKSLLRNPFE AIRPGSAQQV KTGSLLNQPK 1260
AVLQKLAALS DHNPSAPRNS RNFVFHTLSP VKAEAAKESS KSQVKKRGPS FMTSPSPKHL 1320
KTDDSTSGLT RSIFKYLES 1339 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; TAS:Reactome.
 GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
 GO:0033314; P:mitotic DNA replication checkpoint; IMP:UniProtKB.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. 
Interpro
 IPR024147; Claspin.
 IPR024146; Claspin/Claspin-like. 
Pfam
  
SMART
  
PROSITE
  
PRINTS