CDR2_SCHPO - dbPTM
CDR2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDR2_SCHPO
UniProt AC P87050
Protein Name Mitosis inducer protein kinase cdr2
Gene Name cdr2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 775
Subcellular Localization
Protein Description Acts as a mitotic inducer. In G2 it negatively regulates wee1, a mitotic inhibitor. Also has a role in cytokinesis where it required for proper septum formation..
Protein Sequence MSTISEVGPWELGLSLGSGGPNSSRLAKHRETGQLAVVKPIVGWSELTSSQQARIEGELVLLRLIEHPNVLQLIDVISAQEQLFVVVEYMPGGELFDCMLRKGSFTEQDTAKFLWQILCGLEYCHKLHICHRDLKPENLYLDAHGSIKIGEFGMASIQQPGKLLQTSCGSPHYASPEIIMGRSYDGCASDIWSCGIIFFALLTGKLPFDDDNIRSLLLKVCQGQFEMPSNISPQAQHLLYRMLDVDSSTRITMEQIREHPFLSCFVHPNISIPIISAPIQPIDPLIVQHLSLVFRCSDDPMPLYEKLASQSPLVEKTLYTLLSRHLHPPSSAAVDRNRAVVDDLLGTAASNGQQMDEEEIEQAINIPTLAPYPISYAAESVPRPATSASPFLTPVTTSGTFNYSFNATNPQSILQRPATTSSAVPQLPKSVTPGLAYPHDSSMLSSNYRPPSALSPRNFNVSINDPEVQLSRRATSLDMSNDFRMNENDPSIVGNLAASNFPTGMGPPRKRVTSRMSEHTGNRVVSFPRGSAFNPRVTRFNVGNEQFSNNIDNNNYNQPYANATMNNSRRLRTPSGERSMRADLSQSPASYDSLNVPKHRRRQSLFSPSSTKKKLSGSPFQPKRSFLRRLFSSEPSCKCVYASLVASELEHEILEVLRRWQLLGIGIADIIYDSVSASISARIKRQNSLNLKPVRFRISVLAEFFGSQAVFVLESGSSTTFDHLATEFQLIFEDKGFLDNLELSYFQASASRPVSRMSVSSSPFAVFRQRQSVQS
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
166PhosphorylationQPGKLLQTSCGSPHY
CCCCEEHHCCCCCCC
26.4225720772
167PhosphorylationPGKLLQTSCGSPHYA
CCCEEHHCCCCCCCC
11.9729996109
170PhosphorylationLLQTSCGSPHYASPE
EEHHCCCCCCCCCCH
16.9029996109
309PhosphorylationPLYEKLASQSPLVEK
HHHHHHHHCCCHHHH
41.4428889911
311PhosphorylationYEKLASQSPLVEKTL
HHHHHHCCCHHHHHH
20.0828889911
430PhosphorylationAVPQLPKSVTPGLAY
CCCCCCCCCCCCCCC
29.3225720772
432PhosphorylationPQLPKSVTPGLAYPH
CCCCCCCCCCCCCCC
20.8025720772
441PhosphorylationGLAYPHDSSMLSSNY
CCCCCCCHHCCCCCC
18.0229996109
442PhosphorylationLAYPHDSSMLSSNYR
CCCCCCHHCCCCCCC
29.7829996109
446PhosphorylationHDSSMLSSNYRPPSA
CCHHCCCCCCCCCCC
33.6425720772
452PhosphorylationSSNYRPPSALSPRNF
CCCCCCCCCCCCCCE
44.5229996109
455PhosphorylationYRPPSALSPRNFNVS
CCCCCCCCCCCEECC
22.8725720772
462PhosphorylationSPRNFNVSINDPEVQ
CCCCEECCCCCHHHH
19.4425720772
471PhosphorylationNDPEVQLSRRATSLD
CCHHHHHHHHCCCCC
11.5729996109
475PhosphorylationVQLSRRATSLDMSND
HHHHHHCCCCCCCCC
28.1929996109
476PhosphorylationQLSRRATSLDMSNDF
HHHHHCCCCCCCCCC
22.7628889911
480PhosphorylationRATSLDMSNDFRMNE
HCCCCCCCCCCCCCC
32.6829996109
491PhosphorylationRMNENDPSIVGNLAA
CCCCCCHHHHHHHHH
32.5429996109
513PhosphorylationGPPRKRVTSRMSEHT
CCCCHHHCHHCCCCC
18.0429996109
514PhosphorylationPPRKRVTSRMSEHTG
CCCHHHCHHCCCCCC
24.1129996109
517PhosphorylationKRVTSRMSEHTGNRV
HHHCHHCCCCCCCEE
25.7229996109
526PhosphorylationHTGNRVVSFPRGSAF
CCCCEEEECCCCCCC
27.0325720772
573PhosphorylationNNSRRLRTPSGERSM
CCCCCCCCCCCCCCC
26.8029996109
585PhosphorylationRSMRADLSQSPASYD
CCCCCCCCCCCCCHH
29.2025720772
587PhosphorylationMRADLSQSPASYDSL
CCCCCCCCCCCHHHC
21.0328889911
590PhosphorylationDLSQSPASYDSLNVP
CCCCCCCCHHHCCCC
32.6225720772
591PhosphorylationLSQSPASYDSLNVPK
CCCCCCCHHHCCCCH
16.2025720772
593PhosphorylationQSPASYDSLNVPKHR
CCCCCHHHCCCCHHH
17.3825720772
604PhosphorylationPKHRRRQSLFSPSST
CHHHCCCCCCCCCCC
29.5729996109
607PhosphorylationRRRQSLFSPSSTKKK
HCCCCCCCCCCCCCC
29.2129996109
609PhosphorylationRQSLFSPSSTKKKLS
CCCCCCCCCCCCCCC
49.8229996109
610PhosphorylationQSLFSPSSTKKKLSG
CCCCCCCCCCCCCCC
47.8629996109
616PhosphorylationSSTKKKLSGSPFQPK
CCCCCCCCCCCCCCC
46.2129996109
618PhosphorylationTKKKLSGSPFQPKRS
CCCCCCCCCCCCCHH
21.1128889911
632PhosphorylationSFLRRLFSSEPSCKC
HHHHHHHCCCCCCHH
38.0828889911
633PhosphorylationFLRRLFSSEPSCKCV
HHHHHHCCCCCCHHH
46.3129996109
755PhosphorylationASASRPVSRMSVSSS
CCCCCCCCCCCCCCC
25.5829996109
758PhosphorylationSRPVSRMSVSSSPFA
CCCCCCCCCCCCCCH
20.1025720772
760PhosphorylationPVSRMSVSSSPFAVF
CCCCCCCCCCCCHHH
20.1425720772
761PhosphorylationVSRMSVSSSPFAVFR
CCCCCCCCCCCHHHC
39.6229996109
762PhosphorylationSRMSVSSSPFAVFRQ
CCCCCCCCCCHHHCH
19.2725720772

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 CDR2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDR2_SCHPO !!

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 CDR2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CG23_SCHPOcdc13genetic
9843577
CDK1_SCHPOcdc2genetic
9843577
MPIP_SCHPOcdc25genetic
9843577
MPIP_SCHPOcdc25genetic
9843572
WEE1_SCHPOwee1genetic
2245912
CDK1_SCHPOcdc2genetic
2245912
WEE1_SCHPOwee1physical
9843572
MID1_SCHPOmid1physical
22427686
WEE1_SCHPOwee1genetic
9843572
YIQ9_SCHPOSPAC824.09cgenetic
22681890
TCO89_SCHPOtco89genetic
22681890
HAT1_SCHPOhat1genetic
22681890
SWI6_SCHPOswi6genetic
22681890
PPK14_SCHPOppk14genetic
22681890
YEX5_SCHPOptl3genetic
22681890
BDC1_SCHPObdc1genetic
22681890
RL30A_SCHPOrpl3001genetic
22681890
ERG28_SCHPOerg28genetic
22681890
YAA7_SCHPOime4genetic
22681890
MEX67_SCHPOmex67genetic
22681890
MGR2_SCHPOmgr2genetic
22681890
YEPB_SCHPOSPAC23H3.11cgenetic
22681890
VIP1_SCHPOasp1genetic
22681890
TYW2_SCHPOtrm12genetic
22681890
ARP8_SCHPOarp8genetic
22681890
BST1_SCHPObst1genetic
22681890
NEM1_SCHPOnem1genetic
22681890
GYP1_SCHPOgyp1genetic
22681890
YKX4_SCHPOSPAC328.04genetic
22681890
RRG9_SCHPOrrg9genetic
22681890
YEX1_SCHPOSPAC1A6.01cgenetic
22681890
LYS4_SCHPOlys2genetic
22681890
ATPB_SCHPOatp2genetic
22681890
FKBP4_SCHPOfkbp39genetic
22681890
VPS3_SCHPOvps3genetic
22681890
MDV1_SCHPOcaf4genetic
22681890
RAF1_SCHPOraf1genetic
22681890
SSDH1_SCHPOSPAC1002.12cgenetic
22681890
PPID_SCHPOwis2genetic
22681890
MDM31_SCHPOmdm31genetic
22681890
PPK6_SCHPOppk6genetic
22681890
KPR1_SCHPOSPAC4A8.14genetic
22681890
YJC7_SCHPOSPCC736.07cgenetic
22681890
RL21B_SCHPOrpl2102genetic
22681890
PRZ1_SCHPOprz1genetic
22681890
CSK1_SCHPOcsk1genetic
22681890
ARC1_SCHPOSPAC30C2.04genetic
22681890
YIP6_SCHPOSPAC343.06cgenetic
22681890
MEU31_SCHPOmeu31genetic
22681890
YOX1_SCHPOyox1genetic
22681890
BLT1_SCHPOblt1physical
23149940
CUT12_SCHPOcut12genetic
2245912
SSP1_SCHPOssp1physical
24508166
CDR2_SCHPOcdr2physical
24982431
MID1_SCHPOmid1genetic
24982431
MID1_SCHPOmid1physical
26071525
WEE1_SCHPOwee1physical
26071525
MID1_SCHPOmid1genetic
28162898
POM1_SCHPOpom1genetic
28162898

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDR2_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-311; SER-476;SER-587 AND SER-632, AND MASS SPECTROMETRY.

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