CUT12_SCHPO - dbPTM
CUT12_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CUT12_SCHPO
UniProt AC O59755
Protein Name Spindle pole body-associated protein cut12
Gene Name cut12
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 548
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body .
Protein Description Required for bipolar spindle formation. May act as a regulator of the p34cdc2/cyclin B kinase. Required for full activation of the plo1 kinase. However, in cut12.1 cells at restrictive temperature the H1 kinase does rise concomitant with entry into mitosis, indicating that cut12 is not required for activation of p34cdc2/cyclin B. The cut12.s11 allele may promote cdc2-independent phosphorylation of SPB proteins thereby overcoming the requirement for cdc25 in cell cycle progression..
Protein Sequence MSETLNTPPTYAWVLKAFSSKLAGTVTKPVTKMSSYIEDAESDAELPQDAKEDLRPTETLTPLKSKAAQNGILKTPGTLQIKKTVNFKDISKDAATWNRPTKNNFLFTRLDDENPLMGHEEFKSPLLQSTPKPNINNPDNENKSKHDEFDNRYNININESYKNETKSNQRLGEDVPSKKKYPHSMDAEISKFKWDSNNNNDWSSLMKDCFRDVVNNNRKMKEIIKDVMIDTSQAFPSESLDEPDYTINLDAPRSSSGKYWKQKFSMLDSAHSDLELELTSIRERLESLILEKQEEINFWKQRCRALETEKIHNHQGQQSKYKGKEFVGNRFSQMRELYTAKPSPITTKVVSRPSQSDVREPQEQVPSKNLHRGADMSHLAAQMLTHSSKKSHTTNLIPSEGIISSTPISAASKVRMNLMQSNQTPTPAPFSIAAKKSHLPSKLSFPQDGGSLSSATTLQQLPKARVTPNVLSSLSSNLGKTNPTSVYQSKANVTTSADVEKPQVKVATSSRVDYDLKSPNQRTANAKKRLEERRRRRKLKLQELQLNS
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
2Phosphorylation------MSETLNTPP
------CCCCCCCCC		39.0121712547
4Phosphorylation----MSETLNTPPTY
----CCCCCCCCCCH		20.2824763107
7Phosphorylation-MSETLNTPPTYAWV
-CCCCCCCCCCHHHH		33.4824763107
25PhosphorylationFSSKLAGTVTKPVTK
HHCHHCCEECCCCCH		21.2824763107
34PhosphorylationTKPVTKMSSYIEDAE
CCCCCHHHHHHHHHH		22.8821712547
35PhosphorylationKPVTKMSSYIEDAES
CCCCHHHHHHHHHHC		26.9924763107
42PhosphorylationSYIEDAESDAELPQD
HHHHHHHCCCCCCCC		43.7924763107
61PhosphorylationLRPTETLTPLKSKAA
CCCCCCCCCCCCHHH		33.7124763107
75PhosphorylationAQNGILKTPGTLQIK
HHCCCCCCCCEEEEE		24.4124763107
78PhosphorylationGILKTPGTLQIKKTV
CCCCCCCEEEEEEEE		19.3824763107
124PhosphorylationMGHEEFKSPLLQSTP
CCCHHHCCCHHHCCC		26.5424763107
129PhosphorylationFKSPLLQSTPKPNIN
HCCCHHHCCCCCCCC		46.8024763107
130PhosphorylationKSPLLQSTPKPNINN
CCCHHHCCCCCCCCC		23.5221712547
160PhosphorylationYNININESYKNETKS
CCCCCCHHHCCCCCC		36.6029996109
203PhosphorylationSNNNNDWSSLMKDCF
CCCCCCHHHHHHHHH		19.2321712547
339PhosphorylationSQMRELYTAKPSPIT
HHHHHHHHCCCCCCE		40.6129996109
343PhosphorylationELYTAKPSPITTKVV
HHHHCCCCCCEEEEE		28.3829996109
405PhosphorylationPSEGIISSTPISAAS
CCCCCCCCCCCCHHH		28.0024763107
406PhosphorylationSEGIISSTPISAASK
CCCCCCCCCCCHHHH		20.1821712547
409PhosphorylationIISSTPISAASKVRM
CCCCCCCCHHHHHHH		20.9824763107
412PhosphorylationSTPISAASKVRMNLM
CCCCCHHHHHHHHHH		31.2521712547
421PhosphorylationVRMNLMQSNQTPTPA
HHHHHHHCCCCCCCC		19.5529996109
424PhosphorylationNLMQSNQTPTPAPFS
HHHHCCCCCCCCCCC		33.1224763107
431PhosphorylationTPTPAPFSIAAKKSH
CCCCCCCCHHHCCCC		15.4024763107
451PhosphorylationSFPQDGGSLSSATTL
CCCCCCCCCCCCHHH		30.5227738172
453PhosphorylationPQDGGSLSSATTLQQ
CCCCCCCCCCHHHHH		21.4427738172
472PhosphorylationRVTPNVLSSLSSNLG
CCCHHHHHHHHHCCC		25.5821712547
473PhosphorylationVTPNVLSSLSSNLGK
CCHHHHHHHHHCCCC		28.2721712547
475PhosphorylationPNVLSSLSSNLGKTN
HHHHHHHHHCCCCCC		21.0921712547
476PhosphorylationNVLSSLSSNLGKTNP
HHHHHHHHCCCCCCC		41.1721712547
494PhosphorylationYQSKANVTTSADVEK
HHCCCCCCCCCCCCC		18.1629996109
514PhosphorylationATSSRVDYDLKSPNQ
ECCCCCCCCCCCCCH		21.9629996109
518PhosphorylationRVDYDLKSPNQRTAN
CCCCCCCCCCHHHHH		36.0624763107
548PhosphorylationLQELQLNS-------
HHHHHCCC-------		50.6325720772
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 CUT12_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CUT12_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 CUT12_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FIN1_SCHPOfin1genetic
12065422
MPIP_SCHPOcdc25genetic
9531532
CUT12_SCHPOcut12physical
12815070
TFB5_SCHPOtfb5genetic
17409062
MPIP_SCHPOcdc25genetic
17409062
PCP1_SCHPOpcp1physical
22438582
PLO1_SCHPOplo1genetic
12815070
PP11_SCHPOdis2genetic
2245912
PP11_SCHPOdis2physical
23333317
PLO1_SCHPOplo1physical
23333317
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CUT12_SCHPO

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Related Literatures of Post-Translational Modification

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