dbPTM

CDC23_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDC23_HUMAN
UniProt AC	Q9UJX2
Protein Name	Cell division cycle protein 23 homolog
Gene Name	CDC23
Organism	Homo sapiens (Human).
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..
Protein Sequence	MAASTSMVPVAVTAAVAPVLSINSDFSDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLAELQPPPPITEEDAQDMDAYTLAKAYFDVKEYDRAAHFLHGCNSKKAYFLYMYSRYLSGEKKKDDETVDSLGPLEKGQVKNEALRELRVELSKKHQARELDGFGLYLYGVVLRKLDLVKEAIDVFVEATHVLPLHWGAWLELCNLITDKEMLKFLSLPDTWMKEFFLAHIYTELQLIEEALQKYQNLIDVGFSKSSYIVSQIAVAYHNIRDIDKALSIFNELRKQDPYRIENMDTFSNLLYVRSMKSELSYLAHNLCEIDKYRVETCCVIGNYYSLRSQHEKAALYFQRALKLNPRYLGAWTLMGHEYMEMKNTSAAIQAYRHAIEVNKRDYRAWYGLGQTYEILKMPFYCLYYYRRAHQLRPNDSRMLVALGECYEKLNQLVEAKKCYWRAYAVGDVEKMALVKLAKLHEQLTESEQAAQCYIKYIQDIYSCGEIVEHLEESTAFRYLAQYYFKCKLWDEASTCAQKCCAFNDTREEGKALLRQILQLRNQGETPTTEVPAPFFLPASLSANNTPTRRVSPLNLSSVTP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAASTSMVP ------CCCCCCCCC	15.32	22814378
4	Phosphorylation	----MAASTSMVPVA ----CCCCCCCCCHH	16.10	23401153
5	Phosphorylation	---MAASTSMVPVAV ---CCCCCCCCCHHH	19.00	30108239
6	Phosphorylation	--MAASTSMVPVAVT --CCCCCCCCCHHHH	18.45	30108239
13	Phosphorylation	SMVPVAVTAAVAPVL CCCCHHHHHHHHHHH	10.12	30108239
21	Phosphorylation	AAVAPVLSINSDFSD HHHHHHHCCCCCHHH	21.69	23401153
24	Phosphorylation	APVLSINSDFSDLRE HHHHCCCCCHHHHHH	38.06	23401153
25 (in isoform 3)	Ubiquitination	-	42.45	-
27	Phosphorylation	LSINSDFSDLREIKK HCCCCCHHHHHHHHH	40.50	23401153
34	Ubiquitination	SDLREIKKQLLLIAG HHHHHHHHHHHHHHC	52.41	-
43	Phosphorylation	LLLIAGLTRERGLLH HHHHHCHHHCCCCCC	29.57	-
91 (in isoform 1)	Ubiquitination	-	46.89	21906983
93	Phosphorylation	AYTLAKAYFDVKEYD HHHHHHHHHCHHHHH	10.29	29496907
97 (in isoform 2)	Ubiquitination	-	53.02	21906983
97	Ubiquitination	AKAYFDVKEYDRAAH HHHHHCHHHHHHHHH	53.02	21906983
99	Phosphorylation	AYFDVKEYDRAAHFL HHHCHHHHHHHHHHH	12.66	29496907
112	Ubiquitination	FLHGCNSKKAYFLYM HHHCCCCHHHHHHHH	27.68	29967540
115	Phosphorylation	GCNSKKAYFLYMYSR CCCCHHHHHHHHHHH	11.73	26552605
118	Phosphorylation	SKKAYFLYMYSRYLS CHHHHHHHHHHHHHC	5.54	26552605
120	Phosphorylation	KAYFLYMYSRYLSGE HHHHHHHHHHHHCCC	4.04	26552605
121	Phosphorylation	AYFLYMYSRYLSGEK HHHHHHHHHHHCCCC	9.64	26503892
129	Ubiquitination	RYLSGEKKKDDETVD HHHCCCCCCCCCCCC	58.07	29967540
130	Ubiquitination	YLSGEKKKDDETVDS HHCCCCCCCCCCCCC	79.90	29967540
134	Phosphorylation	EKKKDDETVDSLGPL CCCCCCCCCCCCCCC	36.29	23663014
137	Phosphorylation	KDDETVDSLGPLEKG CCCCCCCCCCCCCCC	30.78	23663014
137 (in isoform 1)	Ubiquitination	-	30.78	21906983
141 (in isoform 1)	Ubiquitination	-	11.44	21906983
143	Ubiquitination	DSLGPLEKGQVKNEA CCCCCCCCCHHCHHH	63.43	21906983
147	Sumoylation	PLEKGQVKNEALREL CCCCCHHCHHHHHHH	40.98	-
147	Ubiquitination	PLEKGQVKNEALREL CCCCCHHCHHHHHHH	40.98	21906983
147	Sumoylation	PLEKGQVKNEALREL CCCCCHHCHHHHHHH	40.98	28112733
160	Ubiquitination	ELRVELSKKHQAREL HHHHHHHHHHCCCCC	67.89	27667366
223	Phosphorylation	KEMLKFLSLPDTWMK HHHHHHHCCCCHHHH	40.77	-
267	Phosphorylation	SKSSYIVSQIAVAYH CHHHHHHHHHHHHHH	13.30	14657031
273	Phosphorylation	VSQIAVAYHNIRDID HHHHHHHHHCCCCHH	6.71	22817900
275 (in isoform 1)	Ubiquitination	-	20.51	21906983
281	Ubiquitination	HNIRDIDKALSIFNE HCCCCHHHHHHHHHH	52.11	22817900
284	Phosphorylation	RDIDKALSIFNELRK CCHHHHHHHHHHHHC	29.96	22817900
291	Ubiquitination	SIFNELRKQDPYRIE HHHHHHHCCCCCCCC	72.22	-
302	Phosphorylation	YRIENMDTFSNLLYV CCCCCCCCHHHHHHH	20.42	20068231
304	Phosphorylation	IENMDTFSNLLYVRS CCCCCCHHHHHHHHH	28.76	20068231
308	Phosphorylation	DTFSNLLYVRSMKSE CCHHHHHHHHHHHHH	9.29	20068231
313	Ubiquitination	LLYVRSMKSELSYLA HHHHHHHHHHHHHHH	41.86	21963094
328	Ubiquitination	HNLCEIDKYRVETCC HHHCHHCCCEEEEEE	40.39	-
328	Acetylation	HNLCEIDKYRVETCC HHHCHHCCCEEEEEE	40.39	26051181
329	Phosphorylation	NLCEIDKYRVETCCV HHCHHCCCEEEEEEE	19.02	-
333	Phosphorylation	IDKYRVETCCVIGNY HCCCEEEEEEEECCC	14.35	29978859
335 (in isoform 3)	Ubiquitination	-	3.05	-
340	Phosphorylation	TCCVIGNYYSLRSQH EEEEECCCEECCCHH	6.82	29978859
341	Phosphorylation	CCVIGNYYSLRSQHE EEEECCCEECCCHHH	12.77	29978859
342	Phosphorylation	CVIGNYYSLRSQHEK EEECCCEECCCHHHH	13.62	24719451
345	Phosphorylation	GNYYSLRSQHEKAAL CCCEECCCHHHHHHH	40.98	29978859
349	Ubiquitination	SLRSQHEKAALYFQR ECCCHHHHHHHHHHH	36.51	21963094
353	Phosphorylation	QHEKAALYFQRALKL HHHHHHHHHHHHHHC	7.92	25839225
359	Ubiquitination	LYFQRALKLNPRYLG HHHHHHHHCCHHHHH	45.28	27667366
396	2-Hydroxyisobutyrylation	RHAIEVNKRDYRAWY HHHHHHCHHHHHHHC	52.39	-
396	Ubiquitination	RHAIEVNKRDYRAWY HHHHHHCHHHHHHHC	52.39	22505724
403	Phosphorylation	KRDYRAWYGLGQTYE HHHHHHHCCCCCHHH	11.07	29496907
409	Phosphorylation	WYGLGQTYEILKMPF HCCCCCHHHHHHHHH	7.96	29496907
445	Ubiquitination	ALGECYEKLNQLVEA HHHHHHHHHHHHHHH	26.68	21963094
447 (in isoform 1)	Ubiquitination	-	44.18	21906983
453	Ubiquitination	LNQLVEAKKCYWRAY HHHHHHHHHHHHHHH	29.85	21906983
454	Ubiquitination	NQLVEAKKCYWRAYA HHHHHHHHHHHHHHH	39.34	22817900
460	Phosphorylation	KKCYWRAYAVGDVEK HHHHHHHHHCCCHHH	8.01	-
461 (in isoform 1)	Ubiquitination	-	9.61	21906983
467	Acetylation	YAVGDVEKMALVKLA HHCCCHHHHHHHHHH	29.35	19608861
467	Ubiquitination	YAVGDVEKMALVKLA HHCCCHHHHHHHHHH	29.35	23000965
472	Ubiquitination	VEKMALVKLAKLHEQ HHHHHHHHHHHHHHH	43.51	23000965
475	Ubiquitination	MALVKLAKLHEQLTE HHHHHHHHHHHHCCC	61.89	22817900
522	Methylation	YLAQYYFKCKLWDEA HHHHHHHHCCCHHHH	17.84	-
522	Ubiquitination	YLAQYYFKCKLWDEA HHHHHHHHCCCHHHH	17.84	-
522	Acetylation	YLAQYYFKCKLWDEA HHHHHHHHCCCHHHH	17.84	26051181
524	Ubiquitination	AQYYFKCKLWDEAST HHHHHHCCCHHHHHH	53.88	29967540
530	Phosphorylation	CKLWDEASTCAQKCC CCCHHHHHHHHHHHH	23.21	25159151
535	Acetylation	EASTCAQKCCAFNDT HHHHHHHHHHHCCCC	16.86	26051181
535	Ubiquitination	EASTCAQKCCAFNDT HHHHHHHHHHHCCCC	16.86	21963094
541 (in isoform 1)	Ubiquitination	-	40.46	21906983
542	Phosphorylation	KCCAFNDTREEGKAL HHHHCCCCHHHHHHH	40.87	25159151
547	Ubiquitination	NDTREEGKALLRQIL CCCHHHHHHHHHHHH	38.86	27667366
556	Phosphorylation	LLRQILQLRNQGETP HHHHHHHHHHCCCCC	5.07	22067460
558	Phosphorylation	RQILQLRNQGETPTT HHHHHHHHCCCCCCC	63.90	18669648
559	Phosphorylation	QILQLRNQGETPTTE HHHHHHHCCCCCCCC	44.67	18669648
562	Phosphorylation	QLRNQGETPTTEVPA HHHHCCCCCCCCCCC	32.53	30266825
564	Phosphorylation	RNQGETPTTEVPAPF HHCCCCCCCCCCCCE	42.90	30266825
565	Phosphorylation	NQGETPTTEVPAPFF HCCCCCCCCCCCCEE	35.87	30266825
570	Phosphorylation	PTTEVPAPFFLPASL CCCCCCCCEECCCCC	17.91	22067460
572	Phosphorylation	TEVPAPFFLPASLSA CCCCCCEECCCCCCC	8.54	22067460
576	Phosphorylation	APFFLPASLSANNTP CCEECCCCCCCCCCC	22.40	23401153
578	Phosphorylation	FFLPASLSANNTPTR EECCCCCCCCCCCCC	26.84	30266825
582	Phosphorylation	ASLSANNTPTRRVSP CCCCCCCCCCCCCCC	26.33	30266825
584	Phosphorylation	LSANNTPTRRVSPLN CCCCCCCCCCCCCCC	29.12	30266825
587	Phosphorylation	NNTPTRRVSPLNLSS CCCCCCCCCCCCCCC	6.61	22067460
588	Phosphorylation	NTPTRRVSPLNLSSV CCCCCCCCCCCCCCC	23.12	19664994
590	Phosphorylation	PTRRVSPLNLSSVTP CCCCCCCCCCCCCCC	8.63	22067460
593	Phosphorylation	RVSPLNLSSVTP--- CCCCCCCCCCCC---	22.99	22167270
594	Phosphorylation	VSPLNLSSVTP---- CCCCCCCCCCC----	32.93	22167270
596	Phosphorylation	PLNLSSVTP------ CCCCCCCCC------	25.81	29255136

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
556	T	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
556	T	Phosphorylation	Kinase	PLK1	P53350	PhosphoELM
562	T	Phosphorylation	Kinase	CDK1	P06493	PSP
562	T	Phosphorylation	Kinase	PLK1	P53350	PSP
565	T	Phosphorylation	Kinase	CDK1	P06493	PSP
565	T	Phosphorylation	Kinase	PLK1	P53350	PSP
576	T	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
582	T	Phosphorylation	Kinase	CDK1	P06493	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
562	T	Phosphorylation		14657031
Phosphorylation on Thr-562 occurs specifically during mitosis.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FSBP_HUMAN	RAD54B	physical	16189514
RA54B_HUMAN	RAD54B	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
T22D4_HUMAN	TSC22D4	physical	16189514
CDC27_HUMAN	CDC27	physical	22939629
TRI33_HUMAN	TRIM33	physical	23160376
KDM1A_HUMAN	KDM1A	physical	23455924
SUV91_HUMAN	SUV39H1	physical	23455924
CDC23_HUMAN	CDC23	physical	25416956
OPTN_HUMAN	OPTN	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
FSBP_HUMAN	RAD54B	physical	25416956
RA54B_HUMAN	RAD54B	physical	25416956
APC13_HUMAN	ANAPC13	physical	25416956
GORS2_HUMAN	GORASP2	physical	25416956
PI5PA_HUMAN	INPP5J	physical	25416956
RB15B_HUMAN	RBM15B	physical	25416956
RLP24_HUMAN	RSL24D1	physical	25416956
HEMK1_HUMAN	HEMK1	physical	25416956
NB5R2_HUMAN	CYB5R2	physical	25416956
BCAS3_HUMAN	BCAS3	physical	25416956
IF5A2_HUMAN	EIF5A2	physical	25416956
S52A2_HUMAN	SLC52A2	physical	25416956
CEP44_HUMAN	CEP44	physical	25416956
ATRIP_HUMAN	ATRIP	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
EFC4B_HUMAN	CRACR2A	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
CCD24_HUMAN	CCDC24	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
KCTD6_HUMAN	KCTD6	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
IHO1_HUMAN	CCDC36	physical	25416956
INCA1_HUMAN	INCA1	physical	25416956
APC10_HUMAN	ANAPC10	physical	26344197
APC16_HUMAN	ANAPC16	physical	26344197
APC7_HUMAN	ANAPC7	physical	26344197
CDC16_HUMAN	CDC16	physical	26344197
NP1L1_HUMAN	NAP1L1	physical	26344197
NP1L4_HUMAN	NAP1L4	physical	26344197
TAF4_HUMAN	TAF4	physical	26344197
BUB1B_HUMAN	BUB1B	physical	26496610
CDC20_HUMAN	CDC20	physical	26496610
CDC27_HUMAN	CDC27	physical	26496610
FBRL_HUMAN	FBL	physical	26496610
TZAP_HUMAN	ZBTB48	physical	26496610
NEK2_HUMAN	NEK2	physical	26496610
ZFX_HUMAN	ZFX	physical	26496610
CDC16_HUMAN	CDC16	physical	26496610
NPA1P_HUMAN	URB1	physical	26496610
APC10_HUMAN	ANAPC10	physical	26496610
RPP38_HUMAN	RPP38	physical	26496610
VWA8_HUMAN	VWA8	physical	26496610
APC13_HUMAN	ANAPC13	physical	26496610
APC15_HUMAN	ANAPC15	physical	26496610
EDRF1_HUMAN	EDRF1	physical	26496610
FBX5_HUMAN	FBXO5	physical	26496610
REPI1_HUMAN	REPIN1	physical	26496610
ANC2_HUMAN	ANAPC2	physical	26496610
P5CR2_HUMAN	PYCR2	physical	26496610
APC4_HUMAN	ANAPC4	physical	26496610
CSN7A_HUMAN	COPS7A	physical	26496610
FZR1_HUMAN	FZR1	physical	26496610
APC5_HUMAN	ANAPC5	physical	26496610
APC7_HUMAN	ANAPC7	physical	26496610
YETS2_HUMAN	YEATS2	physical	26496610
F111A_HUMAN	FAM111A	physical	26496610
APC1_HUMAN	ANAPC1	physical	26496610
VKOR1_HUMAN	VKORC1	physical	26496610
OSBL5_HUMAN	OSBPL5	physical	26496610
APC16_HUMAN	ANAPC16	physical	26496610
CDC26_HUMAN	CDC26	physical	26496610
UBP22_HUMAN	USP22	physical	27030811

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CDC23_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; THR-582; SER-588AND THR-596, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562; SER-578; THR-584;SER-588; SER-593 AND THR-596, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578; SER-588AND THR-596, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, ANDMASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Mitotic regulation of the human anaphase-promoting complex byphosphorylation."; Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,Peters J.-M.; EMBO J. 22:6598-6609(2003). Cited for: PHOSPHORYLATION AT TYR-273; THR-562 AND THR-565.	14657031 [Abstract]

show