CDK1_DROME - dbPTM
CDK1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDK1_DROME
UniProt AC P23572
Protein Name Cyclin-dependent kinase 1
Gene Name Cdk1 {ECO:0000312|FlyBase:FBgn0004106}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 297
Subcellular Localization Nucleus.
Protein Description Plays a key role in the control of the eukaryotic cell cycle. [PubMed: 2120044]
Protein Sequence MEDFEKIEKIGEGTYGVVYKGRNRLTGQIVAMKKIRLESDDEGVPSTAIREISLLKELKHENIVCLEDVLMEENRIYLIFEFLSMDLKKYMDSLPVDKHMESELVRSYLYQITSAILFCHRRRVLHRDLKPQNLLIDKSGLIKVADFGLGRSFGIPVRIYTHEIVTLWYRAPEVLLGSPRYSCPVDIWSIGCIFAEMATRKPLFQGDSEIDQLFRMFRILKTPTEDIWPGVTSLPDYKNTFPCWSTNQLTNQLKNLDANGIDLIQKMLIYDPVHRISAKDILEHPYFNGFQSGLVRN
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
6Acetylation--MEDFEKIEKIGEG
--CCCHHHHHCCCCC
57.0421791702
14PhosphorylationIEKIGEGTYGVVYKG
HHCCCCCCCEEEEEC
16.8921082442
15PhosphorylationEKIGEGTYGVVYKGR
HCCCCCCCEEEEECC
20.8421082442
160PhosphorylationFGIPVRIYTHEIVTL
HCCCEEEEECCEEEE
7.4719429919
161PhosphorylationGIPVRIYTHEIVTLW
CCCEEEEECCEEEEE
15.6319429919

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
161TPhosphorylationKinaseCAK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDK1_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 CDK1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNC_DROMECycCphysical
15575970
GLIS2_DROMEsugphysical
15575970
TWINE_DROMEtwephysical
15575970
L2AM_DROMEamdphysical
15575970
CRBN_DROMECG3925physical
15575970
CCNE_DROMECycEphysical
15575970
WEE1_DROMEWee1physical
8573790
CCNB3_DROMECycB3physical
9851980
CKS1_DROMECks30Aphysical
22036573
CCNB3_DROMECycB3physical
22036573
ORC1_DROMEOrc1physical
16188887
ORC2_DROMEOrc2physical
16188887
CKS1_DROMECks30Agenetic
16033797
CCNB_DROMECycBgenetic
24214341
CCNA_DROMECycAgenetic
10320477
Z600_DROMEZ600genetic
17431409
CCNB_DROMECycBphysical
11581162
CCNB_DROMECycBphysical
24214341
CCNB_DROMECycBphysical
8156587
CCNB_DROMECycBphysical
8980229
CCNB_DROMECycBphysical
9851980
CCNA_DROMECycAphysical
17431409
CCNA_DROMECycAphysical
24214341
CCNA_DROMECycAphysical
8156587
CCNA_DROMECycAphysical
8980229
CCNA_DROMECycAphysical
11027291
Z600_DROMEZ600physical
17431409

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDK1_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 THR-14; TYR-15; TYR-160 ANDTHR-161, AND MASS SPECTROMETRY.

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