CDC5L_MOUSE - dbPTM
CDC5L_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC5L_MOUSE
UniProt AC Q6A068
Protein Name Cell division cycle 5-like protein
Gene Name Cdc5l
Organism Mus musculus (Mouse).
Sequence Length 802
Subcellular Localization Nucleus . Nucleus speckle . Cytoplasm . May shuttle between cytoplasm and nucleus.
Protein Description DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR)..
Protein Sequence MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKTAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKKKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEVARQTAEESGITNSASSTLLSEYNVTNNSIALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVTNATPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREIDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKNVGFATNNSEHITYLEHSPYEKFSKEDLKKAQDALVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPAQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLMKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQQRYADLLMEKETLQAKF
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
36PhosphorylationNQWSRIASLLHRKSA
CHHHHHHHHHHHHCH		29.1429176673
225PhosphorylationKKPALGFYDTSEENY
CCCCCCCCCCCHHHH		19.2626643407
227PhosphorylationPALGFYDTSEENYQA
CCCCCCCCCHHHHHH		27.0225159016
228PhosphorylationALGFYDTSEENYQAL
CCCCCCCCHHHHHHH		39.7625159016
232PhosphorylationYDTSEENYQALDADF
CCCCHHHHHHHHHHH		9.8425159016
273PhosphorylationHLKRKKESDLPSAIL
HHHHHHHCCCCHHHH		54.0125521595
277PhosphorylationKKESDLPSAILQTSG
HHHCCCCHHHHHHCC		34.9329899451
294UbiquitinationEFTKKRSKLVLPAPQ
HHHHCCCCEEECCCC		46.80-
303PhosphorylationVLPAPQISDAELQEV
EECCCCCCHHHHHHH		26.0623984901
317PhosphorylationVVKVGQASEVARQTA
HHHHHHHHHHHHHHH		25.3922324799
347PhosphorylationEYNVTNNSIALRTPR
EECCCCCEEEECCCC		16.0025338131
352PhosphorylationNNSIALRTPRTPASQ
CCEEEECCCCCCHHH		20.2626643407
355PhosphorylationIALRTPRTPASQDRI
EEECCCCCCHHHHHH		25.1427087446
358PhosphorylationRTPRTPASQDRILQE
CCCCCCHHHHHHHHH		33.5426643407
373PhosphorylationAQNLMALTNVDTPLK
HHHHHHHHCCCCCCC		24.5325159016
377PhosphorylationMALTNVDTPLKGGLN
HHHHCCCCCCCCCCC		26.6627087446
385PhosphorylationPLKGGLNTPLHESDF
CCCCCCCCCCCCCCC		32.0627087446
390PhosphorylationLNTPLHESDFSGVTP
CCCCCCCCCCCCCCC		32.9627087446
393PhosphorylationPLHESDFSGVTPQRQ
CCCCCCCCCCCCCCE		37.0325619855
396PhosphorylationESDFSGVTPQRQVVQ
CCCCCCCCCCCEEEC		19.7527087446
404PhosphorylationPQRQVVQTPNTVLST
CCCEEECCCCCEECC		13.5922942356
407PhosphorylationQVVQTPNTVLSTPFR
EEECCCCCEECCCCC		24.8328066266
410PhosphorylationQTPNTVLSTPFRTPS
CCCCCEECCCCCCCC		29.6921659605
411PhosphorylationTPNTVLSTPFRTPSN
CCCCEECCCCCCCCC		23.4521659605
415PhosphorylationVLSTPFRTPSNGAEG
EECCCCCCCCCCCCC		31.2923527152
417PhosphorylationSTPFRTPSNGAEGLT
CCCCCCCCCCCCCCC		47.4821659605
424PhosphorylationSNGAEGLTPRSGTTP
CCCCCCCCCCCCCCC		27.7523527152
427PhosphorylationAEGLTPRSGTTPKPV
CCCCCCCCCCCCCCC		41.5125159016
429PhosphorylationGLTPRSGTTPKPVTN
CCCCCCCCCCCCCCC		40.9725159016
430PhosphorylationLTPRSGTTPKPVTNA
CCCCCCCCCCCCCCC		32.6123684622
435PhosphorylationGTTPKPVTNATPGRT
CCCCCCCCCCCCCCC		27.8829472430
438PhosphorylationPKPVTNATPGRTPLR
CCCCCCCCCCCCCCC		28.4826824392
442PhosphorylationTNATPGRTPLRDKLN
CCCCCCCCCCCCCCC		32.3722817900
459PhosphorylationPEDGMADYSDPSYVK
CCCCCCCCCCHHHHH		12.8725159016
460PhosphorylationEDGMADYSDPSYVKQ
CCCCCCCCCHHHHHH		43.5225159016
466UbiquitinationYSDPSYVKQMERESR
CCCHHHHHHHHHHHH		35.38-
769S-nitrosylationAIPRRLECLKEDVQR
CHHHHHHHHHHHHHH		8.5521278135
769S-nitrosocysteineAIPRRLECLKEDVQR
CHHHHHHHHHHHHHH		8.55-
771AcetylationPRRLECLKEDVQRQQ
HHHHHHHHHHHHHHH		64.6222826441
788PhosphorylationEKELQQRYADLLMEK
HHHHHHHHHHHHHHH		10.5020531401
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 CDC5L_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
411TPhosphorylation

-
438TPhosphorylation

-
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 CDC5L_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AQR_HUMANAQRphysical
20360068
U5S1_HUMANEFTUD2physical
20360068
U520_HUMANSNRNP200physical
20360068
CWC15_HUMANCWC15physical
20360068
SYF1_HUMANXAB2physical
20360068
PPIE_HUMANPPIEphysical
20360068
PLRG1_HUMANPLRG1physical
20360068
CRNL1_HUMANCRNKL1physical
20360068
PRP8_HUMANPRPF8physical
20360068
SPF27_HUMANBCAS2physical
20360068
CCD12_HUMANCCDC12physical
20360068
CDC5L_HUMANCDC5Lphysical
20360068
PRP19_HUMANPRPF19physical
20360068
CTBL1_HUMANCTNNBL1physical
20360068
SMD1_HUMANSNRPD1physical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC5L_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-385, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396, ANDMASS SPECTROMETRY.

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