CD11B_MOUSE - dbPTM
CD11B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MGDEKDSWKVKTLD
-CCCHHHHHHHCCHH
39.6020469934
47PhosphorylationDRDSKRDSLEEGELR
CCHHHHHHCHHCCCC
41.5325521595
61PhosphorylationRDHRMEITIRNSPYR
CCCEEEEEECCCCCC
10.6930352176
65PhosphorylationMEITIRNSPYRREDS
EEEEECCCCCCCCCC
17.2926824392
67PhosphorylationITIRNSPYRREDSME
EEECCCCCCCCCCCC
23.3225159016
72PhosphorylationSPYRREDSMEDRGEE
CCCCCCCCCCCCCCC
21.2225159016
113PhosphorylationKEKRRHRSHSAEGGK
HHHHHHHHHCCCCCC
18.7027087446
115PhosphorylationKRRHRSHSAEGGKHA
HHHHHHHCCCCCCCH
29.3027087446
232PhosphorylationKGKVGHWSRSPLRPP
CCCCCCCCCCCCCCC
19.7325266776
234PhosphorylationKVGHWSRSPLRPPRE
CCCCCCCCCCCCCHH
23.8326824392
253AcetylationGDNRKPVKEEKVEER
CCCCCCCCHHHHHHH
69.5523864654
264PhosphorylationVEERDLLSDLQDISD
HHHHHHHHHHHHCCH
43.5022802335
270PhosphorylationLSDLQDISDSERKTS
HHHHHHCCHHHHCCC
43.2927087446
272PhosphorylationDLQDISDSERKTSSA
HHHHCCHHHHCCCCC
32.2917203969
370PhosphorylationESRFDRDSGDSEEGE
HHHCCCCCCCCCCCC
45.4526525534
373PhosphorylationFDRDSGDSEEGEEEV
CCCCCCCCCCCCHHC
40.8626525534
384PhosphorylationEEEVGEGTPQSSAPT
CHHCCCCCCCCCCCC
17.5325293948
387PhosphorylationVGEGTPQSSAPTEGD
CCCCCCCCCCCCCCC
29.6625293948
388PhosphorylationGEGTPQSSAPTEGDY
CCCCCCCCCCCCCCC
32.7825293948
391PhosphorylationTPQSSAPTEGDYVPD
CCCCCCCCCCCCCCC
52.9325293948
395PhosphorylationSAPTEGDYVPDSPAL
CCCCCCCCCCCCCCC
25.4125293948
399PhosphorylationEGDYVPDSPALSPIE
CCCCCCCCCCCCHHH
13.1525293948
403PhosphorylationVPDSPALSPIELKQE
CCCCCCCCHHHHHHH
26.4125293948
423PhosphorylationPALQGCRSVEEFQCL
HHHCCCCCHHHHHHH
37.6528066266
437PhosphorylationLNRIEEGTYGVVYRA
HHCCCCCCCEEEEEE
22.0029176673
471PhosphorylationKEGFPITSLREINTI
HCCCCCCCHHHHHHH
26.58-
477PhosphorylationTSLREINTILKAQHP
CCHHHHHHHHHCCCC
33.09-
553UbiquitinationWILHRDLKTSNLLLS
EEECCCHHHHCCCHH
54.95-
576PhosphorylationDFGLAREYGSPLKAY
CCCHHHHHCCCCCCC
19.8321082442
578PhosphorylationGLAREYGSPLKAYTP
CHHHHHCCCCCCCCC
26.5925521595
583PhosphorylationYGSPLKAYTPVVVTL
HCCCCCCCCCEEEEE
15.2521082442
584PhosphorylationGSPLKAYTPVVVTLW
CCCCCCCCCEEEEEE
17.9226824392
589PhosphorylationAYTPVVVTLWYRAPE
CCCCEEEEEEECCHH
10.4426745281
592PhosphorylationPVVVTLWYRAPELLL
CEEEEEEECCHHHHH
10.4623567750
630UbiquitinationQKPLFPGKSDIDQIN
CCCCCCCCCCHHHHH
45.23-
638UbiquitinationSDIDQINKIFKDLGT
CCHHHHHHHHHHHCC
51.66-
649UbiquitinationDLGTPSEKIWPGYND
HHCCCHHHCCCCCCC
55.17-
662UbiquitinationNDLPAVKKMTFSEYP
CCCHHHHHCCCCCCC
36.25-
740PhosphorylationQQRVKRGTSPRPPEG
HHHHHCCCCCCCCCC
39.3227087446
741PhosphorylationQRVKRGTSPRPPEGG
HHHHCCCCCCCCCCC
23.0327087446
751PhosphorylationPPEGGLGYSQLGDDD
CCCCCCCCHHCCCCC
9.7825521595
752PhosphorylationPEGGLGYSQLGDDDL
CCCCCCCHHCCCCCH
19.6827087446
762PhosphorylationGDDDLKETGFHLTTT
CCCCHHHHCEEEEEC
43.4925777480
767PhosphorylationKETGFHLTTTNQGAS
HHHCEEEEECCCCCC
24.0125777480
768PhosphorylationETGFHLTTTNQGASA
HHCEEEEECCCCCCC
30.0625777480
769PhosphorylationTGFHLTTTNQGASAA
HCEEEEECCCCCCCC
21.9525777480
774PhosphorylationTTTNQGASAAGPGFS
EECCCCCCCCCCCCC
26.0225777480
781PhosphorylationSAAGPGFSLKF----
CCCCCCCCCCC----
36.2425777480

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
471SPhosphorylationKinaseCDK7Q03147
Uniprot
477TPhosphorylationKinaseCDK7Q03147
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
115SPhosphorylation

-

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 CD11B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CD11B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD11B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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