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Q9UJX2 (CDC23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division cycle protein 23 homolog
Alternative name(s):
Anaphase-promoting complex subunit 8
Short name=APC8
Cyclosome subunit 8
Gene names
Name:CDC23
Synonyms:ANAPC8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 12 subunits. Ref.9

Post-translational modification

Phosphorylated. Phosphorylation on Thr-562 occurs specifically during mitosis. Ref.11

Sequence similarities

Belongs to the APC8/CDC23 family.

Contains 9 TPR repeats.

Sequence caution

The sequence AAC70920.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH05258.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH10944.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH17713.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAS99353.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA75628.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD96970.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAF84299.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell cycle

Traceable author statement PubMed 12188893. Source: UniProtKB

metaphase/anaphase transition of mitotic cell cycle

Traceable author statement Ref.8. Source: ProtInc

mitosis

Inferred from direct assay Ref.11. Source: UniProtKB

mitotic G1 phase

Inferred from direct assay PubMed 12629511. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic metaphase plate congression

Inferred from direct assay Ref.11. Source: UniProtKB

mitotic spindle assembly checkpoint

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein K11-linked ubiquitination

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of exit from mitosis

Traceable author statement Ref.8. Source: ProtInc

regulation of mitotic metaphase/anaphase transition

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.8. Source: ProtInc

   Cellular_componentanaphase-promoting complex

Inferred from direct assay Ref.11Ref.22PubMed 21926987. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred from direct assay. Source: LIFEdb

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionubiquitin-protein ligase activity

Traceable author statement PubMed 12629511. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJX2-1)

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.
Isoform 2 (identifier: Q9UJX2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     125-151: SGEKKKDDETVDSLGPLEKGQVKNEAL → VRAILKCHSAFSETSIFRTNGKVKSFK
     152-597: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UJX2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 597596Cell division cycle protein 23 homolog
PRO_0000106270

Regions

Repeat83 – 11634TPR 1
Repeat169 – 20234TPR 2
Repeat228 – 26134TPR 3
Repeat263 – 29634TPR 4
Repeat331 – 36434TPR 5
Repeat366 – 39833TPR 6
Repeat400 – 43233TPR 7
Repeat433 – 46634TPR 8
Repeat468 – 50033TPR 9

Amino acid modifications

Modified residue21N-acetylalanine Ref.21
Modified residue2731Phosphotyrosine Ref.11
Modified residue4671N6-acetyllysine Ref.17
Modified residue5621Phosphothreonine Ref.11 Ref.15
Modified residue5651Phosphothreonine Ref.11
Modified residue5781Phosphoserine Ref.16
Modified residue5821Phosphothreonine Ref.15 Ref.16
Modified residue5881Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.20
Modified residue5931Phosphoserine Ref.15
Modified residue5961Phosphothreonine Ref.12 Ref.15 Ref.16 Ref.18 Ref.20

Natural variations

Alternative sequence1 – 118118Missing in isoform 3.
VSP_037678
Alternative sequence125 – 15127SGEKK…KNEAL → VRAILKCHSAFSETSIFRTN GKVKSFK in isoform 2.
VSP_008429
Alternative sequence152 – 597446Missing in isoform 2.
VSP_008430
Natural variant91P → L.
Corresponds to variant rs2231471 [ dbSNP | Ensembl ].
VAR_024675
Natural variant781E → Q. Ref.3
Corresponds to variant rs17228304 [ dbSNP | Ensembl ].
VAR_019232

Experimental info

Sequence conflict831D → E in BAD96970. Ref.4
Sequence conflict1051F → S in BAD96970. Ref.4
Sequence conflict5271D → G in BAG65414. Ref.2
Sequence conflict5881S → F in AAF05755. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 28, 2009. Version 3.
Checksum: 358F2B8745DB9D32

FASTA59768,834
        10         20         30         40         50         60 
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF 

        70         80         90        100        110        120 
SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY 

       130        140        150        160        170        180 
SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSK KHQARELDGF GLYLYGVVLR 

       190        200        210        220        230        240 
KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE 

       250        260        270        280        290        300 
LQLIEEALQK YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM 

       310        320        330        340        350        360 
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL 

       370        380        390        400        410        420 
NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY 

       430        440        450        460        470        480 
YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL 

       490        500        510        520        530        540 
TESEQAAQCY IKYIQDIYSC GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN 

       550        560        570        580        590 
DTREEGKALL RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP 

« Hide

Isoform 2 [UniParc].

Checksum: 0FE42406F299DAD4
Show »

FASTA15116,821
Isoform 3 [UniParc].

Checksum: 1E4655ABEAAB2D9A
Show »

FASTA47955,882

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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].
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT51168.
RefSeqNP_004652.2. NM_004661.3.
UniGeneHs.73625.

3D structure databases

ProteinModelPortalQ9UJX2.
SMRQ9UJX2. Positions 29-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114242. 52 interactions.
DIPDIP-32959N.
IntActQ9UJX2. 39 interactions.
MINTMINT-1437590.
STRING9606.ENSP00000378350.

PTM databases

PhosphoSiteQ9UJX2.

Polymorphism databases

DMDM254763423.

Proteomic databases

PaxDbQ9UJX2.
PRIDEQ9UJX2.

Protocols and materials databases

DNASU8697.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
ENST00000394886; ENSP00000378350; ENSG00000094880. [Q9UJX2-1]
GeneID8697.
KEGGhsa:8697.
UCSCuc003lcl.3. human. [Q9UJX2-1]
uc003lcm.1. human. [Q9UJX2-2]

Organism-specific databases

CTD8697.
GeneCardsGC05M137552.
H-InvDBHIX0005208.
HGNCHGNC:1724. CDC23.
HPAHPA039593.
MIM603462. gene.
neXtProtNX_Q9UJX2.
PharmGKBPA26258.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOVERGENHBG050858.
InParanoidQ9UJX2.
KOK03355.
OMACDYNDAR.
OrthoDBEOG7TQV0C.
PhylomeDBQ9UJX2.
TreeFamTF101055.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UJX2.
BgeeQ9UJX2.
CleanExHS_CDC23.
GenevestigatorQ9UJX2.

Family and domain databases

Gene3D1.25.40.10. 4 hits.
InterProIPR007192. APC8.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF04049. APC8. 1 hit.
PF00515. TPR_1. 4 hits.
[Graphical view]
SMARTSM00028. TPR. 6 hits.
[Graphical view]
PROSITEPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCDC23.
GenomeRNAi8697.
NextBio32613.
PROQ9UJX2.
SOURCESearch...

Entry information

Entry nameCDC23_HUMAN
AccessionPrimary (citable) accession number: Q9UJX2
Secondary accession number(s): A8K6E5 expand/collapse secondary AC list , B4E3A2, B7WP05, D3DQB7, O75433, Q53FN2, Q9BS73
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM