Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cell division cycle protein 23 homolog  

UniProtKB / Swiss-Prot ID :  CDC23_HUMAN

Gene Name (Synonyms) : 
CDC23, ANAPC8  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  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 MAASTSMVPVAVTAAVAPVLSINSDFSDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLAEL...
Predicted Secondary Structure CCCCHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCHHCCCCCCCC...
Protein Variant
LocationDescription
9P -> L (in dbSNP:rs2231471). VAR_024675
78E -> Q (in dbSNP:rs17228304). VAR_019232
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YFDVKEYDR
HHHHHHHHH
53.02Phosphositeplus
Link-
143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GPLEKGQVK
CCHHHHHHH
63.43Phosphositeplus
Link-
147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGQVKNEAL
HHHHHHHHH
40.98Phosphositeplus
Link-
273PhosphotyrosineIAVAYHNIR
HHCCHHHHH
6.71PhosphoELM
Link-
273PhosphotyrosineIAVAYHNIR
HHCCHHHHH
6.71Phosphositeplus
Link-
273Phosphotyrosine.IAVAYHNIR
HHCCHHHHH
6.71UniProtKB
Link-
281Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RDIDKALSI
HHHHHHHHH
52.11Phosphositeplus
Link-
284PhosphoserineDKALSIFNE
HHHHHHHCC
29.96Phosphositeplus
Link-
304PhosphoserineMDTFSNLLY
HHHHHCCHH
28.76HPRD
Link-
308PhosphotyrosineSNLLYVRSM
HCCHHHHHH
9.29HPRD
Link-
453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVEAKKCYW
HHHHHHHHC
29.85Phosphositeplus
Link-
467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDVEKMALV
HHHHHHHHH
29.35Phosphositeplus
Link-
467N6-acetyllysineGDVEKMALV
HHHHHHHHH
29.35HPRD
Link-
467N6-acetyllysineGDVEKMALV
HHHHHHHHH
29.35Phosphositeplus
Link-
467N6-acetyllysine.GDVEKMALV
HHHHHHHHH
29.35UniProtKB
Link-
530PhosphoserineWDEASTCAQ
HHHHHHHCC
23.21Phosphositeplus
Link-
542PhosphothreonineAFNDTREEG
HHHHHHHHH
40.87Phosphositeplus
Link-
547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)REEGKALLR
HHHHHHHHH
38.86Phosphositeplus
Link-
562PhosphothreonineNQGETPTTE
HHHHHHHHH
32.53HPRD
Link-
562PhosphothreonineNQGETPTTE
HHHHHHHHH
32.53Phosphositeplus
Link-
562PhosphothreonineNQGETPTTE
HHHHHHHHH
32.53SysPTM
Link-
562Phosphothreonine (CDK1;PLK1)NQGETPTTE
HHHHHHHHH
32.53PhosphoELM
Link-
562Phosphothreonine.NQGETPTTE
HHHHHHHHH
32.53UniProtKB
Link-
564PhosphothreonineGETPTTEVP
HHHHHHHCC
42.90HPRD
Link-
564PhosphothreonineGETPTTEVP
HHHHHHHCC
42.90PhosphoELM
Link-
564PhosphothreonineGETPTTEVP
HHHHHHHCC
42.90Phosphositeplus
Link-
565PhosphothreonineETPTTEVPA
HHHHHHCCC
35.87HPRD
Link-
565PhosphothreonineETPTTEVPA
HHHHHHCCC
35.87PhosphoELM
Link-
565PhosphothreonineETPTTEVPA
HHHHHHCCC
35.87Phosphositeplus
Link-
565Phosphothreonine.ETPTTEVPA
HHHHHHCCC
35.87UniProtKB
Link-
576PhosphoserineFLPASLSAN
CCCCCHHHH
22.40HPRD
Link-
576PhosphoserineFLPASLSAN
CCCCCHHHH
22.40PhosphoELM
Link-
576PhosphoserineFLPASLSAN
CCCCCHHHH
22.40Phosphositeplus
Link-
576PhosphoserineFLPASLSAN
CCCCCHHHH
22.40SysPTM
Link-
576Phosphoserine.FLPASLSAN
CCCCCHHHH
22.40UniProtKB
Link-
578PhosphoserinePASLSANNT
CCCHHHHHC
26.84HPRD
Link-
578PhosphoserinePASLSANNT
CCCHHHHHC
26.84PhosphoELM
Link-
578PhosphoserinePASLSANNT
CCCHHHHHC
26.84Phosphositeplus
Link-
578PhosphoserinePASLSANNT
CCCHHHHHC
26.84SysPTM
Link-
578Phosphoserine.PASLSANNT
CCCHHHHHC
26.84UniProtKB
Link-
582PhosphothreonineSANNTPTRR
HHHHCHHCC
26.33HPRD
Link-
582PhosphothreonineSANNTPTRR
HHHHCHHCC
26.33Phosphositeplus
Link-
582Phosphothreonine (CDK1)SANNTPTRR
HHHHCHHCC
26.33PhosphoELM
Link-
582Phosphothreonine.SANNTPTRR
HHHHCHHCC
26.33UniProtKB
Link-
584PhosphothreonineNNTPTRRVS
HHCHHCCCC
29.12HPRD
Link-
584PhosphothreonineNNTPTRRVS
HHCHHCCCC
29.12PhosphoELM
Link-
584PhosphothreonineNNTPTRRVS
HHCHHCCCC
29.12Phosphositeplus
Link-
584PhosphothreonineNNTPTRRVS
HHCHHCCCC
29.12SysPTM
Link-
584Phosphothreonine.NNTPTRRVS
HHCHHCCCC
29.12UniProtKB
Link-
588PhosphoserineTRRVSPLNL
HCCCCCCC
23.12HPRD
Link-
588PhosphoserineTRRVSPLNL
HCCCCCCC
23.12PhosphoELM
Link-
588PhosphoserineTRRVSPLNL
HCCCCCCC
23.12PhosphoELM
Link-
588PhosphoserineTRRVSPLNL
HCCCCCCC
23.12Phosphositeplus
Link-
588PhosphoserineTRRVSPLNL
HCCCCCCC
23.12SysPTM
Link-
588PhosphoserineTRRVSPLNL
HCCCCCCC
23.12SysPTM
Link-
588Phosphoserine.TRRVSPLNL
HCCCCCCC
23.12UniProtKB
Link-
593PhosphoserinePLNLSSVTP
CCC
22.99HPRD
Link-
593PhosphoserinePLNLSSVTP
CCC
22.99PhosphoELM
Link-
593PhosphoserinePLNLSSVTP
CCC
22.99Phosphositeplus
Link-
593PhosphoserinePLNLSSVTP
CCC
22.99SysPTM
Link-
593Phosphoserine.PLNLSSVTP
CCC
22.99UniProtKB
Link-
594PhosphoserineLNLSSVTP
CC
32.93HPRD
Link-
594PhosphoserineLNLSSVTP
CC
32.93Phosphositeplus
Link-
594PhosphoserineLNLSSVTP
CC
32.93SysPTM
Link-
596PhosphothreonineLSSVTP
25.81HPRD
Link-
596PhosphothreonineLSSVTP
25.81Phosphositeplus
Link-
596PhosphothreonineLSSVTP
25.81SysPTM
Link-
596PhosphothreonineLSSVTP
25.81SysPTM
Link-
596Phosphothreonine.LSSVTP
25.81UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
T22D4_HUMANphysical interactionMINT-67439MINT16189514
RA54B_HUMANphysical interactionEBI-755449
intact16189514
RBPMS_HUMANphysical interactionEBI-755605
intact16189514
T22D4_HUMANphysical interactionEBI-757051
intact16189514
RBPMS_HUMANyeast 2-hybridHPRD:07221HPRD16189514
T22D4_HUMANyeast 2-hybridHPRD:07221HPRD16189514
CDC27_HUMANENSP00000209827STRING
UB2D1_HUMANENSP00000209827STRING
CCNB1_HUMANENSP00000209827STRING
ANC5_HUMANENSP00000209827STRING
CDK2_HUMANENSP00000209827STRING
BUB1B_HUMANENSP00000209827STRING
MD2L1_HUMANENSP00000209827STRING
PLK1_HUMANENSP00000209827STRING
UB2E1_HUMANENSP00000209827STRING
CDC2_HUMANENSP00000209827STRING
CDC20_HUMANENSP00000209827STRING
APC10_HUMANENSP00000209827STRING
AURKB_HUMANENSP00000209827STRING
ANC2_HUMANENSP00000209827STRING
ANC4_HUMANENSP00000209827STRING
STK6_HUMANENSP00000209827STRING
CUL1_HUMANENSP00000209827STRING
ANC1_HUMANENSP00000209827STRING
APC11_HUMANENSP00000209827STRING
PTTG1_HUMANENSP00000209827STRING
PTTG2_HUMANENSP00000209827STRING
APC7_HUMANENSP00000209827STRING
CDC16_HUMANENSP00000209827STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures