CLSPN_DROME - dbPTM
CLSPN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLSPN_DROME
UniProt AC Q8IRB5
Protein Name Claspin {ECO:0000312|FlyBase:FBgn0052251}
Gene Name Claspin {ECO:0000312|FlyBase:FBgn0052251}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1465
Subcellular Localization Nucleus .
Protein Description Required for checkpoint signaling in response to DNA replication stress; either resulting from normal embryogenesis or induced by the DNA synthesis inhibitor hydroxyurea (HU). It is not required for the G2 arrest resulting from DNA double strand breaks induced by ionizing irradiation (IR). Necessary for the timely phosphorylation of Cdk1 at the mid-blastula transition. May have a minor role in maintaining genomic stability in mitotic cells..
Protein Sequence MSESLAETAAAAENEEQADDSMEKLVFDEEDEQMVSGEDLLGGKSLIMSDDSEAEDGSQEKPLSPKDRRRRMMDSDQEEDAMDQGNGDSIKNSEDVEEEMVSRPKKKVSAIIDSDNDDEQQAEKKTQKEEGKQPVKSKKKRSQVNQEDQEKPVKSNKTKKAVKNKTQANKAEDDQDNPSKEDKPKKVVKNKKQTNKDGKPQTNEEYDHHQQHEKPAKTQKSKKLAKKQKQQEDDKEDNGTEQEKKKPSPKSKAKKSDKSKIDSLMDNEEDAGEDLKMYQEDQEPQKQKTKKSAKKTNKDSKEESGEDQEHQEQKKPLKKIKLDNIDTKEDKEQIVKPKKMAKKNKQKVLSDDESEENQNEKVDQDHDLKKMSSENELEMGSDKEDQEMQEPPKKAKKNKQRMDSESEDEIPKTESEKITSSPKNKLKGLVDSESEPEETAEEVSPVKNKLKGLVDSESEPELDNPEESAGEQEAPMESALSREKPKKAKVVRESAKKALEGMQAIQSEQQRLHREAHINVPYHQPKPRTLKEFLSRRTINAPLATALAGGSPMPSRQPRKSVGLRMTREELEAYAKLMEDRAKEATEFFKSESESDEEDDSENEEPMELKDNPGVMDEMLDNPKTPEQPKNDTEDMTSQAVIEVPVLGEDKTDDTVGDEAMVADSITEEEPIASTSTAAALKLADNFEIQQETNAKSPSKVCLVTEVVELPKLDLSTINITPSSKPATPKISEVIRQLKIEKSLDESPSLKGDPNMVIDLETGDMFAKKPTGVDDLLNRLMKTREAKKHKTTETVNILTTEHGKLEMSKVSIHLHEEEIAKEPKPGAGYMKMQEHLKTLITKKRMEDLRKKQAEEQEKMAEDEEEGMDVDEEYEPEDKPGYAEVTINEDEEIIDKVDSTAEDDGDAEENKNDADEDPEDNPVEDSEDEKNDSESEQECEANPEPETQTRKKNRIIKAFEDDNSDEDDLDLLQTPKPSNVAPITATQLQLSAHKLFDVETRRTASDEENELLDLCSGQFPQTQMLSSDAPSVDTAVISQIPMTQFGGSSQAADELEGLCSGTFATQLPSQAPTQQPEQQEESEVPAAVANRIVSSDEEAQEDALEVDKPRNKKLTKKRPKKKAKLGFSDDEDSDDEVEEFDEESDAEPVEEIPETFVDYDSEENEIVVEMTKKDRKIRAANFVDKEAELSESEWGSADEDEKNMDEYDIELGDEDQFDRDKLRHELGQIHARKMMDQDIREVRKIKELLFEEEEEGANRQRQFRWKNVEAGFSLDDNRTDNGEGNDGSGDEENEHLWRKIRYEREQLLLEKGLKPEVASPLSTSVINTSNNGNSPAIRRLNIISSKKTTVEVKKNSPFLISKTIAGKQQKSAVRGSFLIRDQQTLSKLAGLTKGTSGDVDAAEGTISVKSAKAKNFVFATLTEEEHENRKRKAADILNSSTETGVNFIKKPKLEPRRDKCLIDQLL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
45PhosphorylationEDLLGGKSLIMSDDS
CCCCCCCEEECCCCC		26.8022817900
49PhosphorylationGGKSLIMSDDSEAED
CCCEEECCCCCCCCC		31.1319429919
52PhosphorylationSLIMSDDSEAEDGSQ
EEECCCCCCCCCCCC		43.6319429919
64PhosphorylationGSQEKPLSPKDRRRR
CCCCCCCCHHHHHHH		38.1322817900
75PhosphorylationRRRRMMDSDQEEDAM
HHHHCCCCHHHHHHH		24.2522817900
89PhosphorylationMDQGNGDSIKNSEDV
HHCCCCCCCCCCHHH		36.5422817900
109PhosphorylationSRPKKKVSAIIDSDN
CCCCCHHEEEECCCC		23.7222817900
114PhosphorylationKVSAIIDSDNDDEQQ
HHEEEECCCCCHHHH		28.0922817900
300PhosphorylationAKKTNKDSKEESGED
HHHHCCCCCCCCCCC		43.5119429919
304PhosphorylationNKDSKEESGEDQEHQ
CCCCCCCCCCCHHHH		48.8819429919
350PhosphorylationKNKQKVLSDDESEEN
HCCCCCCCCCCCHHH		46.1021082442
354PhosphorylationKVLSDDESEENQNEK
CCCCCCCCHHHHHHC		58.1519429919
372PhosphorylationDHDLKKMSSENELEM
HHHHHHHHHHHCCCC		43.3019429919
373PhosphorylationHDLKKMSSENELEMG
HHHHHHHHHHCCCCC		40.7319429919
381PhosphorylationENELEMGSDKEDQEM
HHCCCCCCCHHHHHH		44.1719429919
404PhosphorylationKNKQRMDSESEDEIP
HHHHHCCCCCCCCCC		33.4119429919
406PhosphorylationKQRMDSESEDEIPKT
HHHCCCCCCCCCCCC		55.0619429919
432PhosphorylationKLKGLVDSESEPEET
HHHCCCCCCCCCHHH		35.2319429919
434PhosphorylationKGLVDSESEPEETAE
HCCCCCCCCCHHHHH		63.5019429919
439PhosphorylationSESEPEETAEEVSPV
CCCCCHHHHHHHHCH		37.3919429919
444PhosphorylationEETAEEVSPVKNKLK
HHHHHHHHCHHHHHC		27.5322817900
456PhosphorylationKLKGLVDSESEPELD
HHCCCCCCCCCCCCC		35.2319429919
458PhosphorylationKGLVDSESEPELDNP
CCCCCCCCCCCCCCC		63.5019429919
468PhosphorylationELDNPEESAGEQEAP
CCCCCCCCCCCCCCC		39.6519429919
538PhosphorylationKEFLSRRTINAPLAT
HHHHHCCCCCHHHHH		19.9221082442
551PhosphorylationATALAGGSPMPSRQP
HHHHCCCCCCCCCCC		19.6722817900
555PhosphorylationAGGSPMPSRQPRKSV
CCCCCCCCCCCCCCC		36.9821082442
586PhosphorylationEDRAKEATEFFKSES
HHHHHHHHHHHHCCC		34.1219429919
591PhosphorylationEATEFFKSESESDEE
HHHHHHHCCCCCCCC		40.9919429919
593PhosphorylationTEFFKSESESDEEDD
HHHHHCCCCCCCCCC		49.8719429919
595PhosphorylationFFKSESESDEEDDSE
HHHCCCCCCCCCCCC		60.6519429919
601PhosphorylationESDEEDDSENEEPME
CCCCCCCCCCCCCCC		55.4319429919
625PhosphorylationEMLDNPKTPEQPKND
HHCCCCCCCCCCCCC		33.0619429919
693PhosphorylationNFEIQQETNAKSPSK
HCCCCHHHCCCCCCC		35.8218327897
699PhosphorylationETNAKSPSKVCLVTE
HHCCCCCCCEEEEEE		44.8222668510
721PhosphorylationDLSTINITPSSKPAT
CCCCCCCCCCCCCCC		16.7819429919
723PhosphorylationSTINITPSSKPATPK
CCCCCCCCCCCCCHH		42.2019429919
724PhosphorylationTINITPSSKPATPKI
CCCCCCCCCCCCHHH		43.8119429919
728PhosphorylationTPSSKPATPKISEVI
CCCCCCCCHHHHHHH		33.3719429919
925PhosphorylationEDNPVEDSEDEKNDS
CCCCCCCCCCCCCCC		33.1819429919
932PhosphorylationSEDEKNDSESEQECE
CCCCCCCCHHHHHHH		53.0320450229
934PhosphorylationDEKNDSESEQECEAN
CCCCCCHHHHHHHHC		48.8320450229
963PhosphorylationKAFEDDNSDEDDLDL
HHHCCCCCCHHHHHH		49.7419429919
973PhosphorylationDDLDLLQTPKPSNVA
HHHHHHCCCCCCCCC		33.0023607784
977PhosphorylationLLQTPKPSNVAPITA
HHCCCCCCCCCCCCC		50.4923607784
990PhosphorylationTATQLQLSAHKLFDV
CCCHHHHHHHCCCCC		18.5022817900
1093PhosphorylationAVANRIVSSDEEAQE
HHHHHHCCCCHHHHH		29.6921082442
1094PhosphorylationVANRIVSSDEEAQED
HHHHHCCCCHHHHHH		37.8421082442
1127PhosphorylationKKAKLGFSDDEDSDD
CCCCCCCCCCCCCCH		42.2122817900
1132PhosphorylationGFSDDEDSDDEVEEF
CCCCCCCCCHHHHHC		44.9322817900
1143PhosphorylationVEEFDEESDAEPVEE
HHHCCCCCCCCCHHH		39.8222817900
1189PhosphorylationVDKEAELSESEWGSA
CCHHHHCCCCCCCCC		30.4919429919
1191PhosphorylationKEAELSESEWGSADE
HHHHCCCCCCCCCCC		34.9619429919
1195PhosphorylationLSESEWGSADEDEKN
CCCCCCCCCCCCCCC		33.3519429919
1272PhosphorylationKNVEAGFSLDDNRTD
ECCCCCCCCCCCCCC		29.9430478224
1287PhosphorylationNGEGNDGSGDEENEH
CCCCCCCCCCHHCHH		46.0323607784
1318PhosphorylationGLKPEVASPLSTSVI
CCCHHHCCCCCCCCE		31.3921082442
1321PhosphorylationPEVASPLSTSVINTS
HHHCCCCCCCCEECC		23.2421082442
1333PhosphorylationNTSNNGNSPAIRRLN
ECCCCCCCHHHHHEE		19.6721082442
1355PhosphorylationTVEVKKNSPFLISKT
EEEECCCCCEEEEEE		26.3822817900
1361AcetylationNSPFLISKTIAGKQQ
CCCEEEEEEECCCHH		36.6421791702
1438PhosphorylationKAADILNSSTETGVN
HHHHHHHCCCHHCCC		34.8822817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CLSPN_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLSPN_DROME !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CLSPN_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CLSPN_DROME !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CLSPN_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-49; SER-52;SER-64; SER-75; SER-109; SER-114; SER-350; SER-354; SER-381; SER-404;SER-406; SER-432; SER-434; SER-444; SER-456; SER-458; SER-468;THR-693; SER-963; THR-973; SER-990; SER-1093; SER-1094 AND SER-1287,AND MASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-963, ANDMASS SPECTROMETRY.

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