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Q9UJX2

- CDC23_HUMAN

UniProt

Q9UJX2 - CDC23_HUMAN

Protein

Cell division cycle protein 23 homolog

Gene

CDC23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      Previous versions | rss
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    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

    Pathwayi

    GO - Molecular functioni

    1. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cell cycle Source: UniProtKB
    3. metaphase/anaphase transition of mitotic cell cycle Source: ProtInc
    4. mitotic cell cycle Source: Reactome
    5. mitotic G1 phase Source: UniProtKB
    6. mitotic metaphase plate congression Source: UniProtKB
    7. mitotic nuclear division Source: UniProtKB
    8. mitotic spindle assembly checkpoint Source: Reactome
    9. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    10. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    11. protein K11-linked ubiquitination Source: UniProtKB
    12. regulation of exit from mitosis Source: ProtInc
    13. regulation of mitotic metaphase/anaphase transition Source: UniProtKB
    14. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. ubiquitin-dependent protein catabolic process Source: ProtInc

    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_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.
    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: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1724. CDC23.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. intracellular Source: LIFEdb
    4. nucleoplasm Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26258.

    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 – 5881Phosphoserine6 Publications
    Modified residuei593 – 5931Phosphoserine1 Publication
    Modified residuei596 – 5961Phosphothreonine5 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation on Thr-562 occurs specifically during mitosis.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJX2.
    PaxDbiQ9UJX2.
    PRIDEiQ9UJX2.

    PTM databases

    PhosphoSiteiQ9UJX2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJX2.
    BgeeiQ9UJX2.
    CleanExiHS_CDC23.
    GenevestigatoriQ9UJX2.

    Organism-specific databases

    HPAiHPA039593.

    Interactioni

    Subunit structurei

    The APC/C is composed of at least 12 subunits.1 Publication

    Protein-protein interaction databases

    BioGridi114242. 52 interactions.
    DIPiDIP-32959N.
    IntActiQ9UJX2. 39 interactions.
    MINTiMINT-1437590.
    STRINGi9606.ENSP00000378350.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJX2.
    SMRiQ9UJX2. Positions 29-495.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati83 – 11634TPR 1Add
    BLAST
    Repeati169 – 20234TPR 2Add
    BLAST
    Repeati228 – 26134TPR 3Add
    BLAST
    Repeati263 – 29634TPR 4Add
    BLAST
    Repeati331 – 36434TPR 5Add
    BLAST
    Repeati366 – 39833TPR 6Add
    BLAST
    Repeati400 – 43233TPR 7Add
    BLAST
    Repeati433 – 46634TPR 8Add
    BLAST
    Repeati468 – 50033TPR 9Add
    BLAST

    Sequence similaritiesi

    Belongs to the APC8/CDC23 family.Curated
    Contains 9 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOVERGENiHBG050858.
    InParanoidiQ9UJX2.
    KOiK03355.
    OMAiAHMYTEL.
    OrthoDBiEOG7TQV0C.
    PhylomeDBiQ9UJX2.
    TreeFamiTF101055.

    Family and domain databases

    Gene3Di1.25.40.10. 4 hits.
    InterProiIPR007192. APC8.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    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. Align

    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

    MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH    50
    SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD 100
    RAAHFLHGCN SKKAYFLYMY SRYLSGEKKK DDETVDSLGP LEKGQVKNEA 150
    LRELRVELSK KHQARELDGF GLYLYGVVLR KLDLVKEAID VFVEATHVLP 200
    LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE LQLIEEALQK 250
    YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM 300
    DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA 350
    ALYFQRALKL NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR 400
    AWYGLGQTYE ILKMPFYCLY YYRRAHQLRP NDSRMLVALG ECYEKLNQLV 450
    EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL TESEQAAQCY IKYIQDIYSC 500
    GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN DTREEGKALL 550
    RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP 597
    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.
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831D → E in BAD96970. 1 PublicationCurated
    Sequence conflicti105 – 1051F → S in BAD96970. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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. [Q9UJX2-1]
    GeneIDi8697.
    KEGGihsa:8697.
    UCSCiuc003lcl.3. human. [Q9UJX2-1]
    uc003lcm.1. human. [Q9UJX2-2]

    Polymorphism databases

    DMDMi254763423.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4200.2. [Q9UJX2-1 ]
    PIRi T51168.
    RefSeqi NP_004652.2. NM_004661.3. [Q9UJX2-1 ]
    UniGenei Hs.73625.

    3D structure databases

    ProteinModelPortali Q9UJX2.
    SMRi Q9UJX2. Positions 29-495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114242. 52 interactions.
    DIPi DIP-32959N.
    IntActi Q9UJX2. 39 interactions.
    MINTi MINT-1437590.
    STRINGi 9606.ENSP00000378350.

    PTM databases

    PhosphoSitei Q9UJX2.

    Polymorphism databases

    DMDMi 254763423.

    Proteomic databases

    MaxQBi Q9UJX2.
    PaxDbi Q9UJX2.
    PRIDEi Q9UJX2.

    Protocols and materials databases

    DNASUi 8697.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394884 ; ENSP00000378348 ; ENSG00000094880 . [Q9UJX2-2 ]
    ENST00000394886 ; ENSP00000378350 ; ENSG00000094880 . [Q9UJX2-1 ]
    GeneIDi 8697.
    KEGGi hsa:8697.
    UCSCi uc003lcl.3. human. [Q9UJX2-1 ]
    uc003lcm.1. human. [Q9UJX2-2 ]

    Organism-specific databases

    CTDi 8697.
    GeneCardsi GC05M137552.
    H-InvDB HIX0005208.
    HGNCi HGNC:1724. CDC23.
    HPAi HPA039593.
    MIMi 603462. gene.
    neXtProti NX_Q9UJX2.
    PharmGKBi PA26258.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOVERGENi HBG050858.
    InParanoidi Q9UJX2.
    KOi K03355.
    OMAi AHMYTEL.
    OrthoDBi EOG7TQV0C.
    PhylomeDBi Q9UJX2.
    TreeFami TF101055.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_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_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.

    Miscellaneous databases

    GeneWikii CDC23.
    GenomeRNAii 8697.
    NextBioi 32613.
    PROi Q9UJX2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJX2.
    Bgeei Q9UJX2.
    CleanExi HS_CDC23.
    Genevestigatori Q9UJX2.

    Family and domain databases

    Gene3Di 1.25.40.10. 4 hits.
    InterProi IPR007192. APC8.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF04049. APC8. 1 hit.
    PF00515. TPR_1. 4 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 6 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 6 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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. 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.

    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: October 1, 2014
    This is version 136 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