CRK1_SCHPO - dbPTM
CRK1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRK1_SCHPO
UniProt AC Q12126
Protein Name Serine/threonine-protein kinase crk1
Gene Name crk1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 335
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Protein kinase essential for cell proliferation, where it is required for completion of cytokinesis. Phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II..
Protein Sequence MDIEKSDKWTYVKERKVGEGTYAVVFLGRQKETNRRVAIKKIKVGQFKDGIDISALREIKFLRESRHDNVIELVDVFSTKSNLNIILEFLDSDLEMLIKDKFIVFQPAHIKSWMVMLLRGLHHIHSRFILHRDLKPNNLLISSDGVLKLADFGLSRDFGTPSHMSHQVITRWYRPPELFMGCRSYGTGVDMWSVGCIFAELMLRTPYLPGESDLDQLNVIFRALGTPEPEVIKSMQQLPNYVEMKHIPPPNGGMEALFSAAGHEEIDLLKMMLDYNPYRRPTAQQALEHHYFSALPKPTHPSLLPRKGGEEGIKHVSSDLQRQNNFPMRANIKFV
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
160PhosphorylationGLSRDFGTPSHMSHQ
CCCCCCCCCCHHCHH
22.9329996109
162PhosphorylationSRDFGTPSHMSHQVI
CCCCCCCCHHCHHHH
31.4928889911
165PhosphorylationFGTPSHMSHQVITRW
CCCCCHHCHHHHHCC
12.829857180
170PhosphorylationHMSHQVITRWYRPPE
HHCHHHHHCCCCCHH
19.1225720772
317PhosphorylationEEGIKHVSSDLQRQN
HHHHHHHHHHHHHHC
20.1829996109
318PhosphorylationEGIKHVSSDLQRQNN
HHHHHHHHHHHHHCC
41.0528889911

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
165SPhosphorylationKinaseCDK7-GPS
165SPhosphorylationKinaseCAK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRK1_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 CRK1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK1_SCHPOcsk1genetic
9857180
CSK1_SCHPOcsk1genetic
11226158
CDK1_SCHPOcdc2genetic
2474475
SEP1_SCHPOsep1genetic
15829570
CGM2_SCHPOmcs2physical
9857180
CGM2_SCHPOmcs2physical
10226032
CGM2_SCHPOmcs2physical
15555586
TFB3_SCHPOpmh1physical
15555586
RPB1_SCHPOrpb1physical
20605454
SPB1_SCHPOspb1physical
22508988
CDK9_SCHPOcdk9genetic
22876190
MTO1_SCHPOSPBC30B4.06cgenetic
22681890
MCL1_SCHPOmcl1genetic
22681890
CDK9_SCHPOcdk9genetic
26275777
RPB1_SCHPOrpb1physical
25691663
CDK1_SCHPOcdc2physical
25691663

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRK1_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-162; SER-165 ANDSER-318, AND MASS SPECTROMETRY.
"Fission yeast Csk1 is a CAK-activating kinase (CAKAK).";
Hermand D., Pihlak A., Westerling T., Damagnez V., Vandenhaute J.,Cottarel G., Makela T.P.;
EMBO J. 17:7230-7238(1998).
Cited for: PHOSPHORYLATION AT SER-165.

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