CDC23_MOUSE - dbPTM
CDC23_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC23_MOUSE
UniProt AC Q8BGZ4
Protein Name Cell division cycle protein 23 homolog
Gene Name Cdc23
Organism Mus musculus (Mouse).
Sequence Length 597
Subcellular Localization
Protein Description Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity)..
Protein Sequence MAANSSVVSVAAAATAVPGVSTVADFSDLQEIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLSELQPPPPLTEEDAQDVDAYTLAKAYFDVKEYDRAAHFLHGCNSKKAYFLYMYSRYLSGEKKKDDETVDSLGPLEKGQVKNEALRELRVELSRKHQARGLDGFGLYLYGVVLRKLDLVKEAIDVFVEATHVLPLHWGAWLELCNLITDKEMLKFLSLPDTWMKEFFLAHIYTELQLIEEALQKYQHLIDVGFSKSSYIVSQIAVAYHNIRDIDKALSIFNELRKQDPYRIENMDTFSNLLYVRSMKSELSYLAHNLCEIDKYRVETCCVIGNYYSLRSQHEKAALYFQRALKLNPRYLGAWTLMGHEYMEMKNTSAAIQAYRHAIEVNKRDYRAWYGLGQTYEILKMPFYCLYYYRRAHQLRPNDSRMLVALGECYEKLNQLVEAKKCYWRAYAVGDVEKKALVKLAKLHEQLTESEQAAQCYIKYIQDIYSCGETVEHLEESTAFRYLAQYYFKCKLWDEASTCAQKCCAFNDTREEGKALLRQILQLRNQGETPTSDTPGTFFLPASLSANNTPTRRVSPLNLSSVTP
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
2Acetylation------MAANSSVVS
------CCCCCHHHH		18.49-
22PhosphorylationTAVPGVSTVADFSDL
HCCCCCCCCCCHHHH		19.8028576409
273PhosphorylationVSQIAVAYHNIRDID
HHHHHHHHHCCCCHH		6.71-
460PhosphorylationKKCYWRAYAVGDVEK
HHHHHHHHHCCCHHH		8.0127180971
467AcetylationYAVGDVEKKALVKLA
HHCCCHHHHHHHHHH		43.10-
562PhosphorylationQLRNQGETPTSDTPG
HHHHCCCCCCCCCCC		38.4026824392
564PhosphorylationRNQGETPTSDTPGTF
HHCCCCCCCCCCCEE		46.8026745281
565PhosphorylationNQGETPTSDTPGTFF
HCCCCCCCCCCCEEE		40.4625521595
567PhosphorylationGETPTSDTPGTFFLP
CCCCCCCCCCEEEEE		24.3226745281
570PhosphorylationPTSDTPGTFFLPASL
CCCCCCCEEEEECHH		16.6526745281
576PhosphorylationGTFFLPASLSANNTP
CEEEEECHHCCCCCC		22.4021082442
578PhosphorylationFFLPASLSANNTPTR
EEEECHHCCCCCCCC		26.8421082442
582PhosphorylationASLSANNTPTRRVSP
CHHCCCCCCCCCCCC		26.3325521595
584PhosphorylationLSANNTPTRRVSPLN
HCCCCCCCCCCCCCC		29.1221082442
588PhosphorylationNTPTRRVSPLNLSSV
CCCCCCCCCCCCCCC		23.1227087446
593PhosphorylationRVSPLNLSSVTP---
CCCCCCCCCCCC---		22.9927149854
594PhosphorylationVSPLNLSSVTP----
CCCCCCCCCCC----		32.9323527152
596PhosphorylationPLNLSSVTP------
CCCCCCCCC------		25.8127087446
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 CDC23_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
562TPhosphorylation

-
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 CDC23_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC26_HUMANCDC26physical
20360068
APC13_HUMANANAPC13physical
20360068
CFA97_HUMANCFAP97physical
20360068
ANC2_HUMANANAPC2physical
20360068
SKP1_HUMANSKP1physical
20360068
NEK2_HUMANNEK2physical
20360068
APC5_HUMANANAPC5physical
20360068
CDC16_HUMANCDC16physical
20360068
APC7_HUMANANAPC7physical
20360068
APC1_HUMANANAPC1physical
20360068
APC11_HUMANANAPC11physical
20360068
FBX5_HUMANFBXO5physical
20360068
APC10_HUMANANAPC10physical
20360068
CDC20_HUMANCDC20physical
20360068
APC16_HUMANANAPC16physical
20360068
FZR1_HUMANFZR1physical
20360068
APC4_HUMANANAPC4physical
20360068
BUB1B_HUMANBUB1Bphysical
20360068
MD2L1_HUMANMAD2L1physical
20360068
CDC27_HUMANCDC27physical
20360068
CDC23_HUMANCDC23physical
20360068
ATP5J_HUMANATP5Jphysical
26496610
BASI_HUMANBSGphysical
26496610
BUB1B_HUMANBUB1Bphysical
26496610
CDC20_HUMANCDC20physical
26496610
CDC27_HUMANCDC27physical
26496610
MD2L1_HUMANMAD2L1physical
26496610
NEK2_HUMANNEK2physical
26496610
P5CR1_HUMANPYCR1physical
26496610
TRI27_HUMANTRIM27physical
26496610
RT12_HUMANMRPS12physical
26496610
RREB1_HUMANRREB1physical
26496610
RIR2_HUMANRRM2physical
26496610
ZNF12_HUMANZNF12physical
26496610
NCOA4_HUMANNCOA4physical
26496610
CUL1_HUMANCUL1physical
26496610
CDC16_HUMANCDC16physical
26496610
BUB3_HUMANBUB3physical
26496610
KIF23_HUMANKIF23physical
26496610
VINEX_HUMANSORBS3physical
26496610
APC10_HUMANANAPC10physical
26496610
APC13_HUMANANAPC13physical
26496610
APC15_HUMANANAPC15physical
26496610
FBX5_HUMANFBXO5physical
26496610
TIM13_HUMANTIMM13physical
26496610
ANC2_HUMANANAPC2physical
26496610
P5CR2_HUMANPYCR2physical
26496610
APC4_HUMANANAPC4physical
26496610
FZR1_HUMANFZR1physical
26496610
APC5_HUMANANAPC5physical
26496610
APC7_HUMANANAPC7physical
26496610
PARD3_HUMANPARD3physical
26496610
CFA97_HUMANCFAP97physical
26496610
DEFM_HUMANPDFphysical
26496610
APC1_HUMANANAPC1physical
26496610
TBC15_HUMANTBC1D15physical
26496610
GNPTA_HUMANGNPTABphysical
26496610
RN170_HUMANRNF170physical
26496610
GNPTG_HUMANGNPTGphysical
26496610
SPB12_HUMANSERPINB12physical
26496610
APC16_HUMANANAPC16physical
26496610
KI18B_HUMANKIF18Bphysical
26496610
CDC26_HUMANCDC26physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC23_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 SER-588 AND THR-596, ANDMASS SPECTROMETRY.
"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 THR-562 AND SER-578, ANDMASS SPECTROMETRY.

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