| UniProt ID | CD11B_MOUSE | |
|---|---|---|
| UniProt AC | P24788 | |
| Protein Name | Cyclin-dependent kinase 11B | |
| Gene Name | Cdk11b | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 784 | |
| Subcellular Localization | ||
| Protein Description | Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity-dependent manner. May act as a negative regulator of normal cell cycle progression.. | |
| Protein Sequence | MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHRMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKAHHRKDEKRKEKRRHRSHSAEGGKHARVKEKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKLREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREEYSDKGKVGHWSRSPLRPPRERFEMGDNRKPVKEEKVEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEEGSTSEESEEEEEEEEEEEEEETGSNSEEASEQSAEEVSDEEMSEDEDRENENHILVVPESRFDRDSGDSEEGEEEVGEGTPQSSAPTEGDYVPDSPALSPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLSGVKHLHDNWILHRDLKTSNLLLSHAGILKVGDFGLAREYGSPLKAYTPVVVTLWYRAPELLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGKSDIDQINKIFKDLGTPSEKIWPGYNDLPAVKKMTFSEYPYNNLRKRFGALLSDQGFDLMNKFLTYYPGRRINAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQRVKRGTSPRPPEGGLGYSQLGDDDLKETGFHLTTTNQGASAAGPGFSLKF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MGDEKDSWKVKTLD -CCCHHHHHHHCCHH | 39.60 | 20469934 | |
| 47 | Phosphorylation | DRDSKRDSLEEGELR CCHHHHHHCHHCCCC | 41.53 | 25521595 | |
| 61 | Phosphorylation | RDHRMEITIRNSPYR CCCEEEEEECCCCCC | 10.69 | 30352176 | |
| 65 | Phosphorylation | MEITIRNSPYRREDS EEEEECCCCCCCCCC | 17.29 | 26824392 | |
| 67 | Phosphorylation | ITIRNSPYRREDSME EEECCCCCCCCCCCC | 23.32 | 25159016 | |
| 72 | Phosphorylation | SPYRREDSMEDRGEE CCCCCCCCCCCCCCC | 21.22 | 25159016 | |
| 113 | Phosphorylation | KEKRRHRSHSAEGGK HHHHHHHHHCCCCCC | 18.70 | 27087446 | |
| 115 | Phosphorylation | KRRHRSHSAEGGKHA HHHHHHHCCCCCCCH | 29.30 | 27087446 | |
| 232 | Phosphorylation | KGKVGHWSRSPLRPP CCCCCCCCCCCCCCC | 19.73 | 25266776 | |
| 234 | Phosphorylation | KVGHWSRSPLRPPRE CCCCCCCCCCCCCHH | 23.83 | 26824392 | |
| 253 | Acetylation | GDNRKPVKEEKVEER CCCCCCCCHHHHHHH | 69.55 | 23864654 | |
| 264 | Phosphorylation | VEERDLLSDLQDISD HHHHHHHHHHHHCCH | 43.50 | 22802335 | |
| 270 | Phosphorylation | LSDLQDISDSERKTS HHHHHHCCHHHHCCC | 43.29 | 27087446 | |
| 272 | Phosphorylation | DLQDISDSERKTSSA HHHHCCHHHHCCCCC | 32.29 | 17203969 | |
| 370 | Phosphorylation | ESRFDRDSGDSEEGE HHHCCCCCCCCCCCC | 45.45 | 26525534 | |
| 373 | Phosphorylation | FDRDSGDSEEGEEEV CCCCCCCCCCCCHHC | 40.86 | 26525534 | |
| 384 | Phosphorylation | EEEVGEGTPQSSAPT CHHCCCCCCCCCCCC | 17.53 | 25293948 | |
| 387 | Phosphorylation | VGEGTPQSSAPTEGD CCCCCCCCCCCCCCC | 29.66 | 25293948 | |
| 388 | Phosphorylation | GEGTPQSSAPTEGDY CCCCCCCCCCCCCCC | 32.78 | 25293948 | |
| 391 | Phosphorylation | TPQSSAPTEGDYVPD CCCCCCCCCCCCCCC | 52.93 | 25293948 | |
| 395 | Phosphorylation | SAPTEGDYVPDSPAL CCCCCCCCCCCCCCC | 25.41 | 25293948 | |
| 399 | Phosphorylation | EGDYVPDSPALSPIE CCCCCCCCCCCCHHH | 13.15 | 25293948 | |
| 403 | Phosphorylation | VPDSPALSPIELKQE CCCCCCCCHHHHHHH | 26.41 | 25293948 | |
| 423 | Phosphorylation | PALQGCRSVEEFQCL HHHCCCCCHHHHHHH | 37.65 | 28066266 | |
| 437 | Phosphorylation | LNRIEEGTYGVVYRA HHCCCCCCCEEEEEE | 22.00 | 29176673 | |
| 471 | Phosphorylation | KEGFPITSLREINTI HCCCCCCCHHHHHHH | 26.58 | - | |
| 477 | Phosphorylation | TSLREINTILKAQHP CCHHHHHHHHHCCCC | 33.09 | - | |
| 553 | Ubiquitination | WILHRDLKTSNLLLS EEECCCHHHHCCCHH | 54.95 | - | |
| 576 | Phosphorylation | DFGLAREYGSPLKAY CCCHHHHHCCCCCCC | 19.83 | 21082442 | |
| 578 | Phosphorylation | GLAREYGSPLKAYTP CHHHHHCCCCCCCCC | 26.59 | 25521595 | |
| 583 | Phosphorylation | YGSPLKAYTPVVVTL HCCCCCCCCCEEEEE | 15.25 | 21082442 | |
| 584 | Phosphorylation | GSPLKAYTPVVVTLW CCCCCCCCCEEEEEE | 17.92 | 26824392 | |
| 589 | Phosphorylation | AYTPVVVTLWYRAPE CCCCEEEEEEECCHH | 10.44 | 26745281 | |
| 592 | Phosphorylation | PVVVTLWYRAPELLL CEEEEEEECCHHHHH | 10.46 | 23567750 | |
| 630 | Ubiquitination | QKPLFPGKSDIDQIN CCCCCCCCCCHHHHH | 45.23 | - | |
| 638 | Ubiquitination | SDIDQINKIFKDLGT CCHHHHHHHHHHHCC | 51.66 | - | |
| 649 | Ubiquitination | DLGTPSEKIWPGYND HHCCCHHHCCCCCCC | 55.17 | - | |
| 662 | Ubiquitination | NDLPAVKKMTFSEYP CCCHHHHHCCCCCCC | 36.25 | - | |
| 740 | Phosphorylation | QQRVKRGTSPRPPEG HHHHHCCCCCCCCCC | 39.32 | 27087446 | |
| 741 | Phosphorylation | QRVKRGTSPRPPEGG HHHHCCCCCCCCCCC | 23.03 | 27087446 | |
| 751 | Phosphorylation | PPEGGLGYSQLGDDD CCCCCCCCHHCCCCC | 9.78 | 25521595 | |
| 752 | Phosphorylation | PEGGLGYSQLGDDDL CCCCCCCHHCCCCCH | 19.68 | 27087446 | |
| 762 | Phosphorylation | GDDDLKETGFHLTTT CCCCHHHHCEEEEEC | 43.49 | 25777480 | |
| 767 | Phosphorylation | KETGFHLTTTNQGAS HHHCEEEEECCCCCC | 24.01 | 25777480 | |
| 768 | Phosphorylation | ETGFHLTTTNQGASA HHCEEEEECCCCCCC | 30.06 | 25777480 | |
| 769 | Phosphorylation | TGFHLTTTNQGASAA HCEEEEECCCCCCCC | 21.95 | 25777480 | |
| 774 | Phosphorylation | TTTNQGASAAGPGFS EECCCCCCCCCCCCC | 26.02 | 25777480 | |
| 781 | Phosphorylation | SAAGPGFSLKF---- CCCCCCCCCCC---- | 36.24 | 25777480 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 115 | S | Phosphorylation |
| - |
* 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 CD11B_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CD11B_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-264; SER-270;THR-740 AND SER-741, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-740 AND SER-741, ANDMASS SPECTROMETRY. | |
| "Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY. | |
| "Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY. | |