CDC11_SCHPO - dbPTM
CDC11_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC11_SCHPO
UniProt AC O74473
Protein Name Septation initiation network scaffold protein cdc11
Gene Name cdc11
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1045
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Localizes at the spindle pole body and the barrier septum.
Protein Description Essential for the onset of septum formation. Involved in the organization of astral microtubules during mitosis. Acts as a bridge between sid4 and the other SIN proteins mediating their association with the spindle pole body (SPB). The sid4-cdc11 complex organizes a signaling hub on the SPB which coordinates cell and nuclear division..
Protein Sequence MEQLWLEHDLSEEWIPQPQEQGSDNSSEPPTTSNVNNTQSTGRGSSGTSTEHGTFKKGRNDAPDVPQWKQVNAKNPVARDIFARLDLENMFEESSKQSPPSKSPTKNPSKKSSNNSSRRSSSSVGKLSNVSNMQSSPSKDPFVSQDYEKESISSSQFSKKYSEGSLKSQQSNTRSNSVHEKQNTDHASNASSSSSVVSSPSLKPNNTSPLKLFQGASDPFTREHLNQLTQDVKSNSFENGEKQFSLPEPRRPQKPMRTTERKASLNTKDLYQEVEEVMARLRGRMPNSGRESTIFLPRKLSGLREEEEQDEISVEVSQEDSSNAFPSLSDQLHLKSLQSMKRVTSIFNDNDDSFPSASSSPQRQAYMTDKMPLREIDVGSSQSSSKTARLNSSPKSTLKTSSVKTRRSHSAQSSRKVSDYPNMVVITPADLPEGIDTTQGSMEFDRIHNRWRRKGHDSDLGFDFETDEDASLSHPERTILFKAASTRHQANNDPNNLEKQQPHSFPLRKQNVAQSEFPKHSLRDNSENAPQILSSFHDLSLQNESFDEMFNGRYENGSPIPFISSGSGLKSKADKDAEYSFSVSRQSIIQILSDVEPYEPFWKRIIQLDISRRHLDSLIGLSELCPSIEELTLEGNEIAYLTGCPVTIRDLNAVENRLSSLTSFSNLLNLQYLDISYNQLEDLTGLSSLIHLRELKVDSNHLWSLDGIQHLDGLLKLSACNNRIKELSFTNSNLHRLEELLLGNNEIEEIEEISSLQNLMVLQLDNNKLTNLKASQPMIHLRILRISNNAIHQLEVDQFPHLRTLYMDLNRFNRPPDIRRLKRLVNFSFRTQDPEASNFVIQPSLDIRNLYLSNNTFVTLDCKHMFLGVRYLELANVQLKEVPKYIATSMPNLRVLDLSHNYISDIESLKPLQMIHRLYLVGNRIKKMRNLCDILANLKQLNVLDLRMNPLNFNIYPVIDDSIYELSAASKYQQSINQKGHHRKEDPQKQWQEKELAFSSTLSEAWRTRRKMYAEAILLACPHLEWLDGSDVSQSSRAAFTKSSN
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
54PhosphorylationGTSTEHGTFKKGRND
CCCCCCCCCCCCCCC		33.9029996109
94PhosphorylationLENMFEESSKQSPPS
HHHHHHHHHCCCCCC		35.3229996109
98PhosphorylationFEESSKQSPPSKSPT
HHHHHCCCCCCCCCC		42.3829996109
101PhosphorylationSSKQSPPSKSPTKNP
HHCCCCCCCCCCCCC		49.5029996109
103PhosphorylationKQSPPSKSPTKNPSK
CCCCCCCCCCCCCCC		41.9829996109
131PhosphorylationVGKLSNVSNMQSSPS
HHHHHCCCCCCCCCC		30.7329996109
135PhosphorylationSNVSNMQSSPSKDPF
HCCCCCCCCCCCCCC		33.1924763107
136PhosphorylationNVSNMQSSPSKDPFV
CCCCCCCCCCCCCCC		19.1221712547
138PhosphorylationSNMQSSPSKDPFVSQ
CCCCCCCCCCCCCCC		52.1921712547
144PhosphorylationPSKDPFVSQDYEKES
CCCCCCCCCCCCHHC		20.0821712547
162PhosphorylationSQFSKKYSEGSLKSQ
HHHHHHHCCCCCCCC		44.3424763107
165PhosphorylationSKKYSEGSLKSQQSN
HHHHCCCCCCCCCCC		28.6824763107
168PhosphorylationYSEGSLKSQQSNTRS
HCCCCCCCCCCCCCC		38.4521712547
171PhosphorylationGSLKSQQSNTRSNSV
CCCCCCCCCCCCCCH		32.3121712547
173PhosphorylationLKSQQSNTRSNSVHE
CCCCCCCCCCCCHHH		40.5021712547
175PhosphorylationSQQSNTRSNSVHEKQ
CCCCCCCCCCHHHHC		31.2721712547
199PhosphorylationSSSSVVSSPSLKPNN
CCCCCCCCCCCCCCC		13.6021712547
207PhosphorylationPSLKPNNTSPLKLFQ
CCCCCCCCCCCHHCC		38.0621712547
288PhosphorylationLRGRMPNSGRESTIF
HCCCCCCCCCCCEEE		33.1025720772
292PhosphorylationMPNSGRESTIFLPRK
CCCCCCCCEEEECHH		25.9925720772
353PhosphorylationIFNDNDDSFPSASSS
HHCCCCCCCCCCCCC		41.7525720772
356PhosphorylationDNDDSFPSASSSPQR
CCCCCCCCCCCCHHH		38.4824763107
358PhosphorylationDDSFPSASSSPQRQA
CCCCCCCCCCHHHHH		35.3725720772
359PhosphorylationDSFPSASSSPQRQAY
CCCCCCCCCHHHHHH		45.8424763107
360PhosphorylationSFPSASSSPQRQAYM
CCCCCCCCHHHHHHH		23.6628889911
380PhosphorylationLREIDVGSSQSSSKT
CCCCCCCCCCCCCCC		25.6721712547
381PhosphorylationREIDVGSSQSSSKTA
CCCCCCCCCCCCCCC		28.3121712547
383PhosphorylationIDVGSSQSSSKTARL
CCCCCCCCCCCCCCC		38.2324763107
384PhosphorylationDVGSSQSSSKTARLN
CCCCCCCCCCCCCCC		28.3721712547
387PhosphorylationSSQSSSKTARLNSSP
CCCCCCCCCCCCCCC		20.9621712547
392PhosphorylationSKTARLNSSPKSTLK
CCCCCCCCCCCCCCC		53.2424763107
393PhosphorylationKTARLNSSPKSTLKT
CCCCCCCCCCCCCCC		34.9621712547
458PhosphorylationWRRKGHDSDLGFDFE
HHHCCCCCCCCCCCC		29.1221712547
466PhosphorylationDLGFDFETDEDASLS
CCCCCCCCCCCCCCC		44.6921712547
471PhosphorylationFETDEDASLSHPERT
CCCCCCCCCCCCCCE		42.6021712547
485PhosphorylationTILFKAASTRHQANN
EEEHHHHHHHHHHCC		30.7324763107
554PhosphorylationDEMFNGRYENGSPIP
HHHHCCCCCCCCCCC		18.3625720772
558PhosphorylationNGRYENGSPIPFISS
CCCCCCCCCCCEECC		31.1028889911
580PhosphorylationADKDAEYSFSVSRQS
CCCCCCEEEEECHHH		11.5329996109
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 CDC11_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDC11_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 CDC11_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPG1_SCHPOspg1genetic
9649519
2AD1_SCHPOpar1genetic
11707284
ZFS1_SCHPOzfs1genetic
10462526
IMP2_SCHPOimp2genetic
9786952
DIMI_SCHPOdim1genetic
9182666
SCW1_SCHPOscw1genetic
12242222
PP2B_SCHPOppb1genetic
12354095
SCE3_SCHPOsce3genetic
9254700
ACE2_SCHPOace2genetic
16415366
PPC89_SCHPOppc89physical
16775007
SID4_SCHPOsid4physical
11676915
CG23_SCHPOcdc13physical
15062098
CDK1_SCHPOcdc2physical
15062098
SID4_SCHPOsid4physical
11950932
CDC11_SCHPOcdc11physical
15132994
BYR4_SCHPObyr4physical
12546793
CDC7_SCHPOcdc7genetic
1527180
CDC14_SCHPOcdc14genetic
1527180
RCC1_SCHPOpim1genetic
12446769
CDC16_SCHPOcdc16genetic
1527180
CDC15_SCHPOcdc15genetic
1527180
2ABA_SCHPOpab1genetic
20876564
GEF2_SCHPOgef2genetic
22298427
PTPA2_SCHPOypa2genetic
22267499
PP2A2_SCHPOppa2genetic
22267499
YNVD_SCHPOfar10genetic
22119525
YEYA_SCHPOcsc4genetic
22119525
PLO1_SCHPOplo1genetic
10924454
CDC7_SCHPOcdc7genetic
10924454
SPG1_SCHPOspg1genetic
10924454
SCE3_SCHPOsce3genetic
10924454
RHO1_SCHPOrho1genetic
10924454
TPM_SCHPOcdc8genetic
10924454
SCW1_SCHPOscw1genetic
12796296
FLP1_SCHPOclp1physical
23297348
SID1_SCHPOsid1genetic
23297348
SPG1_SCHPOspg1genetic
23297348
CDC7_SCHPOcdc7genetic
23297348
CDC11_SCHPOcdc11physical
23695164
CDC11_SCHPOcdc11physical
26771498
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC11_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-360 AND SER-558, ANDMASS SPECTROMETRY.

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