Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division cycle protein 23 homolog

Gene

CDC23

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 23 homolog
Alternative name(s):
Anaphase-promoting complex subunit 8
Short name:
APC8
Cyclosome subunit 8
Gene namesi
Name:CDC23
Synonyms:ANAPC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:1724. CDC23.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • intracellular Source: LIFEdb
  • nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26258.

Polymorphism and mutation databases

BioMutaiCDC23.
DMDMi254763423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 597596Cell division cycle protein 23 homologPRO_0000106270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei273 – 2731Phosphotyrosine1 Publication
Modified residuei467 – 4671N6-acetyllysine1 Publication
Modified residuei562 – 5621Phosphothreonine2 Publications
Modified residuei565 – 5651Phosphothreonine1 Publication
Modified residuei578 – 5781Phosphoserine1 Publication
Modified residuei582 – 5821Phosphothreonine2 Publications
Modified residuei588 – 5881Phosphoserine7 Publications
Modified residuei593 – 5931Phosphoserine1 Publication
Modified residuei596 – 5961Phosphothreonine6 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation on Thr-562 occurs specifically during mitosis.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UJX2.
PaxDbiQ9UJX2.
PRIDEiQ9UJX2.

PTM databases

PhosphoSiteiQ9UJX2.

Expressioni

Gene expression databases

BgeeiQ9UJX2.
CleanExiHS_CDC23.
ExpressionAtlasiQ9UJX2. baseline and differential.
GenevisibleiQ9UJX2. HS.

Organism-specific databases

HPAiHPA039593.

Interactioni

Subunit structurei

The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANAPC13A8K3Z63EBI-396137,EBI-10322710
APOL1O147913EBI-396137,EBI-1221934
ATRIPQ8WXE13EBI-396137,EBI-747353
BCAS3Q9H6U63EBI-396137,EBI-6083685
BYSLQ138955EBI-396137,EBI-358049
CCDC24Q8N4L83EBI-396137,EBI-1104933
CCDC36Q8IYA83EBI-396137,EBI-8638439
CEP44Q9C0F13EBI-396137,EBI-744115
COILP384323EBI-396137,EBI-945751
CRACR2AQ9BSW23EBI-396137,EBI-739773
CYB5R2Q6BCY43EBI-396137,EBI-744761
EIF5A2Q9GZV43EBI-396137,EBI-748028
FAM9BQ8IZU03EBI-396137,EBI-10175124
FLJ34048A4D1I33EBI-396137,EBI-10173415
FSBPO950733EBI-396137,EBI-1059030
GORASP2Q9H8Y83EBI-396137,EBI-739467
HEMK1Q9Y5R43EBI-396137,EBI-10329202
INCA1Q0VD863EBI-396137,EBI-6509505
INPP5JQ157353EBI-396137,EBI-10236940
KCTD6Q8NC693EBI-396137,EBI-2511344
LZTS2Q9BRK43EBI-396137,EBI-741037
OPTNQ96CV94EBI-396137,EBI-748974
PNMA5Q96PV43EBI-396137,EBI-10171633
RAC1P630003EBI-396137,EBI-413628
RBM15BQ8NDT2-23EBI-396137,EBI-10269922
RBPMSQ930624EBI-396137,EBI-740322
RSL24D1Q9UHA33EBI-396137,EBI-749321
SIAH1Q8IUQ43EBI-396137,EBI-747107
SLC52A2Q9HAB33EBI-396137,EBI-10309896
SOX5P357113EBI-396137,EBI-3505701
SPERTQ8NA613EBI-396137,EBI-741724
SSX2IPQ9Y2D83EBI-396137,EBI-2212028
TRIM27P143734EBI-396137,EBI-719493

Protein-protein interaction databases

BioGridi114242. 91 interactions.
DIPiDIP-32959N.
IntActiQ9UJX2. 71 interactions.
MINTiMINT-1437590.
STRINGi9606.ENSP00000378350.

Structurei

3D structure databases

ProteinModelPortaliQ9UJX2.
SMRiQ9UJX2. Positions 29-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 6337TPR 1Add
BLAST
Repeati73 – 11240TPR 2Add
BLAST
Repeati114 – 14431TPR 3Add
BLAST
Repeati169 – 20032TPR 4Add
BLAST
Repeati229 – 25931TPR 5Add
BLAST
Repeati263 – 29331TPR 6Add
BLAST
Repeati297 – 32731TPR 7Add
BLAST
Repeati331 – 36131TPR 8Add
BLAST
Repeati366 – 39530TPR 9Add
BLAST
Repeati400 – 43233TPR 10Add
BLAST
Repeati433 – 46634TPR 11Add
BLAST
Repeati468 – 50033TPR 12Add
BLAST
Repeati504 – 54037TPR 13Add
BLAST

Sequence similaritiesi

Belongs to the APC8/CDC23 family.Curated
Contains 13 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00550000074886.
HOVERGENiHBG050858.
InParanoidiQ9UJX2.
KOiK03355.
OMAiCWIKDFF.
OrthoDBiEOG7TQV0C.
PhylomeDBiQ9UJX2.
TreeFamiTF101055.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04049. APC8. 1 hit.
PF00515. TPR_1. 4 hits.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UJX2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH
60 70 80 90 100
SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD
110 120 130 140 150
RAAHFLHGCN SKKAYFLYMY SRYLSGEKKK DDETVDSLGP LEKGQVKNEA
160 170 180 190 200
LRELRVELSK KHQARELDGF GLYLYGVVLR KLDLVKEAID VFVEATHVLP
210 220 230 240 250
LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE LQLIEEALQK
260 270 280 290 300
YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
310 320 330 340 350
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA
360 370 380 390 400
ALYFQRALKL NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR
410 420 430 440 450
AWYGLGQTYE ILKMPFYCLY YYRRAHQLRP NDSRMLVALG ECYEKLNQLV
460 470 480 490 500
EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL TESEQAAQCY IKYIQDIYSC
510 520 530 540 550
GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN DTREEGKALL
560 570 580 590
RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP
Length:597
Mass (Da):68,834
Last modified:July 28, 2009 - v3
Checksum:i358F2B8745DB9D32
GO
Isoform 2 (identifier: Q9UJX2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-151: SGEKKKDDETVDSLGPLEKGQVKNEAL → VRAILKCHSAFSETSIFRTNGKVKSFK
     152-597: Missing.

Note: No experimental confirmation available.
Show »
Length:151
Mass (Da):16,821
Checksum:i0FE42406F299DAD4
GO
Isoform 3 (identifier: Q9UJX2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Note: No experimental confirmation available.
Show »
Length:479
Mass (Da):55,882
Checksum:i1E4655ABEAAB2D9A
GO

Sequence cautioni

The sequence AAC70920.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH05258.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH10944.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH17713.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAS99353.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA75628.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD96970.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAF84299.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831D → E in BAD96970 (Ref. 4) Curated
Sequence conflicti105 – 1051F → S in BAD96970 (Ref. 4) Curated
Sequence conflicti527 – 5271D → G in BAG65414 (PubMed:14702039).Curated
Sequence conflicti588 – 5881S → F in AAF05755 (PubMed:9469815).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91P → L.
Corresponds to variant rs2231471 [ dbSNP | Ensembl ].
VAR_024675
Natural varianti78 – 781E → Q.1 Publication
Corresponds to variant rs17228304 [ dbSNP | Ensembl ].
VAR_019232

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 3. 1 PublicationVSP_037678Add
BLAST
Alternative sequencei125 – 15127SGEKK…KNEAL → VRAILKCHSAFSETSIFRTN GKVKSFK in isoform 2. 1 PublicationVSP_008429Add
BLAST
Alternative sequencei152 – 597446Missing in isoform 2. 1 PublicationVSP_008430Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011472 mRNA. Translation: BAA75628.1. Different initiation.
AK291610 mRNA. Translation: BAF84299.1. Different initiation.
AK304635 mRNA. Translation: BAG65414.1.
AY603103 Genomic DNA. Translation: AAS99353.1. Different initiation.
AK223250 mRNA. Translation: BAD96970.1. Different initiation.
AC106752 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62155.1.
CH471062 Genomic DNA. Translation: EAW62154.1.
CH471062 Genomic DNA. Translation: EAW62156.1.
BC005258 mRNA. Translation: AAH05258.1. Different initiation.
BC010944 mRNA. Translation: AAH10944.1. Different initiation.
BC017713 mRNA. Translation: AAH17713.1. Different initiation.
AF053977 mRNA. Translation: AAC70920.1. Different initiation.
AF191341 mRNA. Translation: AAF05755.1.
BT009810 mRNA. Translation: AAP88812.1.
CCDSiCCDS4200.2. [Q9UJX2-1]
PIRiT51168.
RefSeqiNP_004652.2. NM_004661.3. [Q9UJX2-1]
UniGeneiHs.73625.

Genome annotation databases

EnsembliENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
ENST00000394886; ENSP00000378350; ENSG00000094880.
GeneIDi8697.
KEGGihsa:8697.
UCSCiuc003lcl.3. human. [Q9UJX2-1]
uc003lcm.1. human. [Q9UJX2-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011472 mRNA. Translation: BAA75628.1. Different initiation.
AK291610 mRNA. Translation: BAF84299.1. Different initiation.
AK304635 mRNA. Translation: BAG65414.1.
AY603103 Genomic DNA. Translation: AAS99353.1. Different initiation.
AK223250 mRNA. Translation: BAD96970.1. Different initiation.
AC106752 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62155.1.
CH471062 Genomic DNA. Translation: EAW62154.1.
CH471062 Genomic DNA. Translation: EAW62156.1.
BC005258 mRNA. Translation: AAH05258.1. Different initiation.
BC010944 mRNA. Translation: AAH10944.1. Different initiation.
BC017713 mRNA. Translation: AAH17713.1. Different initiation.
AF053977 mRNA. Translation: AAC70920.1. Different initiation.
AF191341 mRNA. Translation: AAF05755.1.
BT009810 mRNA. Translation: AAP88812.1.
CCDSiCCDS4200.2. [Q9UJX2-1]
PIRiT51168.
RefSeqiNP_004652.2. NM_004661.3. [Q9UJX2-1]
UniGeneiHs.73625.

3D structure databases

ProteinModelPortaliQ9UJX2.
SMRiQ9UJX2. Positions 29-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114242. 91 interactions.
DIPiDIP-32959N.
IntActiQ9UJX2. 71 interactions.
MINTiMINT-1437590.
STRINGi9606.ENSP00000378350.

PTM databases

PhosphoSiteiQ9UJX2.

Polymorphism and mutation databases

BioMutaiCDC23.
DMDMi254763423.

Proteomic databases

MaxQBiQ9UJX2.
PaxDbiQ9UJX2.
PRIDEiQ9UJX2.

Protocols and materials databases

DNASUi8697.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
ENST00000394886; ENSP00000378350; ENSG00000094880.
GeneIDi8697.
KEGGihsa:8697.
UCSCiuc003lcl.3. human. [Q9UJX2-1]
uc003lcm.1. human. [Q9UJX2-2]

Organism-specific databases

CTDi8697.
GeneCardsiGC05M137552.
H-InvDBHIX0005208.
HGNCiHGNC:1724. CDC23.
HPAiHPA039593.
MIMi603462. gene.
neXtProtiNX_Q9UJX2.
PharmGKBiPA26258.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00550000074886.
HOVERGENiHBG050858.
InParanoidiQ9UJX2.
KOiK03355.
OMAiCWIKDFF.
OrthoDBiEOG7TQV0C.
PhylomeDBiQ9UJX2.
TreeFamiTF101055.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Miscellaneous databases

ChiTaRSiCDC23. human.
GeneWikiiCDC23.
GenomeRNAii8697.
NextBioi32613.
PROiQ9UJX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJX2.
CleanExiHS_CDC23.
ExpressionAtlasiQ9UJX2. baseline and differential.
GenevisibleiQ9UJX2. HS.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04049. APC8. 1 hit.
PF00515. TPR_1. 4 hits.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human CDC23 gene."
    Oyamatsu T., Kotani S., Todokoro K.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Placenta and Uterus.
  3. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-78.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Gastric mucosa.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-597 (ISOFORM 1).
    Tissue: Brain, Duodenum and Pancreas.
  8. "Human CDC23: cDNA cloning, mapping to 5q31, genomic structure, and evaluation as a candidate tumor suppressor gene in myeloid leukemias."
    Zhao N., Lai F., Fernald A.A., Eisenbart J.D., Espinosa R., Wang P.W., Le Beau M.M.
    Genomics 53:184-190(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-597 (ISOFORM 1).
    Tissue: Bone marrow.
  9. "Identification of a cullin homology region in a subunit of the anaphase-promoting complex."
    Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.
    Science 279:1219-1222(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-597 (ISOFORM 1), SUBUNIT.
  10. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-597 (ISOFORM 1).
  11. "Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
    Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
    EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-273; THR-562 AND THR-565.
  12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
    Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
    Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE APC/C.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562; THR-582; SER-588; SER-593 AND THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; THR-582; SER-588 AND THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Structural basis for the subunit assembly of the anaphase-promoting complex."
    Schreiber A., Stengel F., Zhang Z., Enchev R.I., Kong E.H., Morris E.P., Robinson C.V., da Fonseca P.C., Barford D.
    Nature 470:227-232(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TPR REPEATS.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
    Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
    Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE APC/C.
  25. "Molecular architecture and mechanism of the anaphase-promoting complex."
    Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.
    Nature 513:388-393(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, SUBUNIT.

Entry informationi

Entry nameiCDC23_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX2
Secondary accession number(s): A8K6E5
, B4E3A2, B7WP05, D3DQB7, O75433, Q53FN2, Q9BS73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: July 28, 2009
Last modified: July 22, 2015
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.